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2'-C-methyl-ATP + RNAn
diphosphate + RNAn+1
-
misincorporation frequency of approximately 1 in 7800 2'-C-methyl-ATP
-
-
?
2'-deoxy-ATP + RNAn
diphosphate + RNAn+1
-
misincorporation
-
-
?
3'-deoxy-ATP + RNAn
diphosphate + RNAn+1
-
misincorporation frequency of approximately 1 in 5 3'-dATP
-
-
?
ATP + RNAn
diphosphate + RNAn+1
CTP + RNAn
diphosphate + RNAn+1
d(Ap4T) + RNAn
?
-
primer elongation
-
-
?
d(TP4C) + RNAn
?
-
primer elongation
-
-
?
d(Tp4G) + RNAn
?
-
primer elongation
-
-
?
d(Tp4T) + RNAn
?
-
primer elongation
-
-
?
dGTP + RNAn
diphosphate + RNAn+1
-
-
-
-
?
DNA + 5-[[(2-aminoethyl)amino]carbonyl]-UTP
?
-
-
-
-
?
DNA + 5-[[(2-methylpropyl)amino]carbonyl]-UTP
?
-
-
-
-
?
DNA + 5-[[(2-pyridinylmethyl)amino]carbonyl]-UTP
?
-
-
-
-
?
DNA + 5-[[(4-pyridinylmethyl)amino]carbonyl]-UTP
?
-
-
-
-
?
DNA + 5-[[benzylamino]carbonyl]-UTP
?
-
-
-
-
?
DNA + 5-[[[2-(1H-imidazol-4-yl)ethyl]amino]carbonyl]-UTP
?
-
-
-
-
?
DNA + 5-[[[2-(1H-indol-3-yl)ethyl]amino]carbonyl]-1-deazaUTP
?
-
-
-
-
?
dTTP + RNAn
?
-
primer elongation
-
-
?
dUTP + RNAn
diphosphate + RNAn+1
-
-
-
-
?
GTP + RNAn
diphosphate + RNAn+1
nucleoside triphosphate + A10G2A2C2C
?
-
oligonucleotide extension
-
-
?
nucleoside triphosphate + A9G3A2C2C
?
-
oligonucleotide extension
-
-
?
nucleoside triphosphate + G2CAC2C
?
-
oligonucleotide extension
-
-
?
nucleoside triphosphate + promoter complex
?
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
nucleoside triphosphate + T10G2T2C2C
?
-
oligonucleotide extension
-
-
?
rGTP + RNAn
diphosphate + RNAn+1
-
-
-
-
?
rNTP + RNAn
diphosphate + RNAn+1
Vectrevirus K1E
-
-
-
?
rUTP + RNAn
diphosphate + RNAn+1
-
-
-
-
?
UTP + RNAn
diphosphate + RNAn+1
-
-
-
-
?
additional information
?
-
ATP + RNAn
diphosphate + RNAn+1
-
-
-
-
?
ATP + RNAn
diphosphate + RNAn+1
-
-
-
-
?
ATP + RNAn
diphosphate + RNAn+1
-
-
-
?
ATP + RNAn
diphosphate + RNAn+1
the primer can be extended only in the presence of ATP. The length of the double-stranded region of RNA/DNA duplexes is important for the primer extension. The length of the double-stranded region of RNA/DNA duplexes is important for the primer extension performed by the enzyme. Under these in vitro conditions POLRMT has a preference for P/T duplexes with short hybridization regions
-
-
?
ATP + RNAn
diphosphate + RNAn+1
-
-
-
-
?
ATP + RNAn
diphosphate + RNAn+1
-
-
-
-
?
CTP + RNAn
diphosphate + RNAn+1
-
-
-
-
?
CTP + RNAn
diphosphate + RNAn+1
-
-
-
-
?
CTP + RNAn
diphosphate + RNAn+1
-
-
-
-
?
GTP + RNAn
diphosphate + RNAn+1
-
-
-
-
?
GTP + RNAn
diphosphate + RNAn+1
-
-
-
-
?
GTP + RNAn
diphosphate + RNAn+1
-
-
-
-
?
GTP + RNAn
diphosphate + RNAn+1
-
-
-
-
?
GTP + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme requires DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme requires DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme requires DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
Autographa californica M nucleopolyhedrovirus transcribes genes using two DNA-directed RNA polymerases. Early genes are transcribed by the host RNA polymerase II, and late and very late genes are transcribed by a viral-encoded multisubunit RNA polymerase
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
RNAP is an exceptionally complex enzyme that can be thought of as the engine of gene expression, synthesis of RNA transcripts of many thousands of nucleotides without dissociation. Energy, in the form of nucleoside triphosphates, fuels the synthesis of an RNA polymer complementary to specific regions of the DNA template. Like all macromolecular synthesis, RNA synthesis can be divided into three general phases: initiation, elongation, and termination. Importantly, each of these phases can be a target of regulation. Promoter recognition, binding at the extended promoter recognition region, and transcript initiation, RNAP prefers to initiate transcription within a narrow window located between 6 and 9 bp downstream of the -10 element, promoter clearance and elongation, termination and recycling, mechanisms and regulation , overview. The process of start site selection can be governed by the availability of either the +1 or the +2 NTP, depending on the promoter
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
DNA templates containing smaller base modifications in 2'-deoxyribonucleoside triphosphates (H, Me in 7-deazapurines) are perfectly tolerated whereas bulky modifications (Ph at any nucleobase) and uracil blocked transcription. Some middle-sized modifications (vinyl or ethynyl) are partly tolerated. In all cases where the transcription proceeds, full length RNA product with correct sequence is obtained indicating that the modifications of the template are not mutagenic and the inhibition is probably at the stage of initiation
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme requires DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme requires DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
absolutely dependent on the presence of a double-stranded or single-stranded DNA template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
with poly(dA-dT) DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme requires DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
denatured calf-thymus DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme requires DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
transcription elongation as a critical regulatory step in addition to initiation
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
various DNA lesions significantly affect the efficiency and fidelity of RNA synthesis. DNA modifications that disrupt correct base-pairing can strongly inhibit transcription and increase nucleotide misincorporation by RNAP. The universal transcription factor GreA and Deinococcus-specific factor Gfh1 stimulate RNAP stalling at various DNA lesions, depending on the type of the lesion and the presence of Mn2+ ions
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
DNA-template dependent reaction. T7 DNA and the plasmid PBR322 are by far the best templates. P2, T4 and T5 DNA are weak templates
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
DNA-template dependent reaction. T7 DNA and the plasmid PBR322 are by far the best templates. P2, T4 and T5 DNA are weak templates
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
template is DNA
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme requires DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
a kind of transcription complex is formed during RNA polymerase catalysed synthesis of the M13 bacteriophage replication primer. The complex contains an overextended RNADNA hybrid bound in the RNA-polymerase through that is normally occupied by downstream double-stranded DNA, thus leaving the 30 end of the RNA available for interaction with DNA polymerase
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
enzyme is responsible for transcription in bacteria
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
regulation by anions, overview
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
RNAP is an exceptionally complex enzyme that can be thought of as the engine of gene expression, synthesis of RNA transcripts of many thousands of nucleotides without dissociation. Energy, in the form of nucleoside triphosphates, fuels the synthesis of an RNA polymer complementary to specific regions of the DNA template. Like all macromolecular synthesis, RNA synthesis can be divided into three general phases: initiation, elongation, and termination. Importantly, each of these phases can be a target of regulation. Promoter recognition, binding at the extended promoter recognition region, and transcript initiation, RNAP prefers to initiate transcription within a narrow window located between 6 and 9 bp downstream of the -10 element, promoter clearance and elongation, termination and recycling, mechanisms and regulation , overview. The process of start site selection can be governed by the availability of either the +1 or the +2 NTP, depending on the promoter
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
template is DNA
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
template is DNA, native or denatured, method evaluation: specificity and extent of transcription depends strongly on the quality of the DNA preparation, the strength of the promoter and terminator sequences, and the kind and concentration of mono- and divalent cations in the reaction mixture
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
template is supercoiled DNA
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
the alpha subunit C-terminal domain of Escherichia coli RNA polymerase (alphaCTD) recognizes the upstream promoter(UP) DNA element via its characteristic minor groove shape and electrostatic potential
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
the alpha subunit C-terminal domain of Escherichia coli RNA polymerase (alphaCTD) recognizes the upstream promoter(UP) DNA element via its characteristic minor groove shape and electrostatic potential
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the catalytic specificity for ribonucleoside triphosphates vs. deoxynucleoside triphosphates during transcript elongation is 80
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme requires DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
mediates fast promoter-independent extension of unstable nucleic acid complexes
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
short DNA or RNA substrates are good substrates for the enzyme
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
substrate specifically binds to the enzyme in the open conformation, where it is base paired with the acceptor template base, while Tyr639 provides discrimination of ribose versus deoxyribose substrates. Substrate selection occurs prior to the isomerization to the catalytically active conformation
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the single subunit DNA-dependent RNA polymerase from bacteriophage T7 catalyzes both promoterdependent transcription initiation and promoter-independent elongation
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
mechanism for de novo RNA synthesis, transcription begins with a marked preference for GTP at the +1 and +2 positions
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
T7 RNAP undergoes a slow conformational change to form an elongation competent complex with the promoter-free substrate. The complex binds to a correct NTP and incorporates the nucleoside monophosphate into RNA primer very efficiently. In the presence of inorganic pyrophosphate, the elongation complex catalyzes the reverse pyrophosphorolysis reaction at a maximum rate of 0.8 per s
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
two proton transfer occurs in the transition state for nucleotidyl-transfer reaction. Associative-like transition-state structure
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
template is DNA
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme requires DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme requires DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the hepatitis delta virus is an RNA virus that depends on DNA-dependent RNA polymerase for its transcription and replication. The association between human RNAP II and hepatitis delta virus RNA suggest two transcription start sites on both polarities of hepatitis delta virus RNA
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
RNAPIIis recruited to gene promoters in a hypo-phosphorylated state
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
template is DNA
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
template is DNA, epigenetic control of rDNA transcription, regulation system of RNA polymerase, detailed overview
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
DNA supercoiling-dependent and LSP-dependent RNA synthesis, three templates are used for in vitro RNA synthesis: the run-off template contains the light strand promoter, conserved sequence blocks, and heavy-strand origin. Promoter-independent RNA synthesis is dependent on DNA supercoiling and on TFB2M
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
in vitro transcription reactions with ATP, CTP, 3'-methyl-GTP, UTP, and DNA
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
Inovirus M13
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
Inovirus M13
-
minimal M13 origin hairpin is bound in the RNAP core channel normally occupied by dsDNA downstream of the transcription initiation start site, the sigma subunit is not required for initiation of RNA synthesis but it is essential for escape into productive elongation, RNAP recognition of the M13 ori and mechanism of RNA synthesis during transcription, detailed overview. During transcription elongation, RNAP can processively synthesize RNAs for thousands of nt. Mechanism of priming on dsDNA, overview
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme requires DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme requires DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
the enzyme requires DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme requires DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
template is DNA
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
template is DNA, epigenetic control of rDNA transcription, regulation system of RNA polymerase, detailed overview
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
in vitro transcription with calf thymus DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
in vitro transcription with calf thymus DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme requires DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
DNA-directed RNA polymerase activity
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
supercoiled, double-stranded DNA template is more efficient than that from nonsupercoiled DNA, in vitro transcription activity and mechanism, overview
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme requires DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme is able to use a variety of DNA templates. DNA from bacteriphage phiPLS27 is transcribed more efficiently than DNA isolated from lamda or herring sperm. DNA isolated from bacteriophage T7 and T7 D111 is utilized more efficiently
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme requires DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
recruitment of the enzyme is a rate-limiting step for the activation of the sigma(54) promoter Pu of Pseudomonas putida, overview
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme requires DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme requires DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
in vitro transcription reactions with ATP, CTP, GTP, UTP, and oligo(dC)-tailed DNA template derived from pAd-GR220
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme requires DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme requires DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
template is DNA
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
template is DNA, RNA translation process and mechanism of DNA-damage recognition by Pol II, detailed overview
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
template is plasmid DNA
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
Rpo41 and Rpo41-Mtf1 synthesize RNA on M13 ssDNA template
30-nt and 41-nt products of Rpo41 and 30-nt, 41-nt, and 60-nt products of Rpo41-Mtf1
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme requires DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme requires DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme requires DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
DNA-template dependent reaction. The best of the templates is phiH DNA, whereas T7 and T4 DNA are comparatively inactive and P2 DNA is a very weak template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
DNA-template dependent reaction. The best of the templates is phiH DNA, whereas T7 and T4 DNA are comparatively inactive and P2 DNA is a very weak template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme requires DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
DNA-template dependent reaction. The enzyme transcribes phiH DNA as efficiently and T4 DNA as weakly as the Sulfolobus enzyme but T7 DNA even better than phiH DNA
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
DNA-template dependent reaction. The enzyme transcribes phiH DNA as efficiently and T4 DNA as weakly as the Sulfolobus enzyme but T7 DNA even better than phiH DNA
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme requires DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme is highly active with poly dAT or T7 phage DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme can bind to DNA containing the lambdaPR promoter, form an open complex and initiate transcription in a temperature-dependent manner. The organism relies on the high temperature of its environment to provide the thermal energy required to stimulate open promoter complex formation, initiate transcription, and facilitate the conformational changes in RNA polymerase that results in nucleotide incorporation
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
calf thymus DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme requires DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
calf thymus DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme requires DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme can bind to DNA containing the lambdaPR promoter, form an open complex and initiate transcription in a temperature-dependent manner. The organism relies on the high temperature of its environment to provide the thermal energy required to stimulate open promoter complex formation, initiate transcription, and facilitate the conformational changes in RNA polymerase that results in nucleotide incorporation
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme requires DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
higher error ratios in transcription by RNA polymerase II are observed in the presence of Mn2+ compared to Mg2+. RNA polymerase II is able to elongate a primer with a 3'-terminal mismatch and thus to incorporate the mismatched nucleotide stable in the nascent RNA
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme requires DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme requires DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
nucleoside triphosphate phosphohydrolase I binds to the H4L subunit of virion RNA polymerase. These observation provides an explanation that UUUUUNU-dependent transcription termination is restricted to early genes, whose transcription is catalyzed by the H4L-containing virion RNA polymerase
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme requires DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
nucleoside triphosphate phosphohydrolase I binds to the H4L subunit of virion RNA polymerase. These observation provides an explanation that UUUUUNU-dependent transcription termination is restricted to early genes, whose transcription is catalyzed by the H4L-containing virion RNA polymerase
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme requires DNA as template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
Zindervirus SP6
-
template is DNA
-
-
?
additional information
?
-
-
dinucleoside teraphosphates are more potent substrates than dinucleoside triphosphates and dinucleoside pentaphosphates
-
-
?
additional information
?
-
-
multi-subunit DNA-dependent RNA polymerases synthesize RNA molecules thousands of nucleotides long. The reiterative reaction of nucleotide condensation occurs at rates of tens of nucleotides per second, invariably linked to the translocation of the enzyme along the DNA template, or threading of the DNA and the nascent RNA molecule through the enzyme. Reiteration of the nucleotide addition/translocation cycle without dissociation from the DNA and RNA requires both isomorphic and metamorphic conformational flexibility of a magnitude substantial enough to accommodate the requisite molecular motions
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-
?
additional information
?
-
-
RNAP adds nucleotides to the 3'-end of the growing RNA and translocates reiteratively, in single nucleotide steps. Translocation mechanism models, concerning conformational changes, allosteric effects and isomerization, and model evaluation, overview
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?
additional information
?
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the core enzyme, which lacks the sigma subunit, synthesizes short transcripts relatively uniformly on the DNA template in the presence of high concentrations of random primers and low NTP concentrations
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additional information
?
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dsDNA templates used for activity are T7A1_763, T7A1_437, T7A1_149, pcDNA3.1, pGEM, T-phage DNA, Escherichia coli DNA, calf thymus DNA, poly(dA-dT), and Kool NC-45
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additional information
?
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RNA polymerase binds multiple sites in the ehxCABD gene regulatory region. At the Escherichia coli ehxCABD operon, RNA polymerase is unable to distinguish between the promoter -10 element and similar overlapping sequences. RNA polymerase competes with itself for binding to AT-rich sequences overlapping PehxCABD, correct positioning of RNA polymerase at PehxCABD requires H-NS
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?
additional information
?
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the subunits interact with recombinant His6-tagged CedA, a multi-copy suppressor which represses the dnaAcos inhibition of cell division. Determination of the binding site of CedA for RNA polymerase. The N-terminus of CedA is necessary for a tight interaction
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additional information
?
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molecular mechanisms of transcription regulation in mitochondria, molecular organization of the human mitochondrial transcription initiation complex, overview
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?
additional information
?
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RNA pol III transcribes structural RNAs involved in RNA processing, U6 snRNA, and translation, tRNA. Mechanism of regulation of RNA pol III transcription by BRCA1, overview
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?
additional information
?
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RNA polymerase II phosphorylation during paused, active and poised transcription cycles with in itiation and elongation stages and at different phosphorylation stages, RNA polymerase II and histone modification profiles across genes in paused, active and poised states, and RNAPII regulation mechanisms at active genes, detailed overview. In embryonic stem cells, silent developmental regulator genes that are repressed by Polycomb are associated with a form of RNAPII that can elongate through coding regions but that lacks the post-translational modifications that are important for coupling RNA synthesis to co-transcriptional maturation
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?
additional information
?
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TLS regulates both RNAPs II and III and supports the possibility that cross-regulation between RNA polymerases is important in maintaining normal cell growth
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?
additional information
?
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two distinct forms, Pol Ialpha and Pol Ibeta. Both forms are catalytically active, but only Pol Ibeta can assemble into productive transcription initiation complexes. Regulation of Pol I transcription during cell cycle progression involving cytokines, and structural organization of mammalian rDNA repeats and the basal factors required for transcription initiation, overview. The activity of basal Pol I factors is regulated by posttranslational modifications
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additional information
?
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negative DNA supercoiling favors the induction of unpaired regions at some sequence motifs on dsDNA, substrate specificity and structural effects on activity, overview
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additional information
?
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RNA polymerase III transcribes small untranslated RNAs that include tRNAs, 5S RNA, U6 RNA, and some microRNAs
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?
additional information
?
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the B2 family of short interspersed elements is transcribed into non-coding RNA by RNA polymerase III
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additional information
?
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POLRMT can act as a primase in vitro and support lagging-strand DNA synthesis on a small 70 bp minicircle, overview
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additional information
?
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incorporation of 2'-dATP or 2'-F-ATP does not lead to immediate chain termination, but the enzyme can not add the second 2'-dATP or 2'-F-ATP to the synthesized RNA
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additional information
?
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incorporation of 2'-dATP or 2'-F-ATP does not lead to immediate chain termination, but the enzyme can not add the second 2'-dATP or 2'-F-ATP to the synthesized RNA
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additional information
?
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Inovirus M13
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multisubunit RNA polymerase transcribes DNA, but is also known to synthesize DNA replication primers in the replication system, a function that is commonly performed by primases, mechanism of primer synthesis by RNA polymerase and comparison to the mechanism of both types of primases, overview
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?
additional information
?
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RNAP II participates in the generation of mRNAs and most of the small nuclear RNAs, while RNAP III synthesizes small essential RNAs, such as tRNAs, 5S rRNA and some snRNAs
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?
additional information
?
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RNAP II participates in the generation of mRNAs and most of the small nuclear RNAs, while RNAP III synthesizes small essential RNAs, such as tRNAs, 5S rRNA and some snRNAs
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?
additional information
?
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active site structure formed by amino acids from two domains: Palm with Asp457 and Asp695, and Fingers with Tyr537 and Lys529, overview
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?
additional information
?
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intermittent hypoxia, a major pathological factor in the development of neural deficits associated with sleep-disordered breathing, regulates RNA polymerase II in hippocampus and prefrontal cortex. Chronic intermittent hypoxia, but not sustained hypoxia, stimulates hydroxylation of Pro1465 in large subunit of RNA polymerase II and phosphorylation of Ser5 of Rpb1, specifically in the CA1 region of the hippocampus and in the prefrontal cortex but not in other regions of the brain, requiring the von Hippel-Lindau tumor suppressor. Mice exposed to chronic IH demonstrated cognitive deficits related to dysfunction in those brain regions, overview
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?
additional information
?
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two distinct forms, Pol Ialpha and Pol Ibeta. Both forms are catalytically active, but only Pol Ibeta can assemble into productive transcription initiation complexes. Regulation of Pol I transcription during cell cycle progression involving cytokines, and structural organization of mammalian rDNA repeats and the basal factors required for transcription initiation, overview. The activity of basal Pol I factors is regulated by posttranslational modifications
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additional information
?
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the enzyme binds to the iNOS promoter
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additional information
?
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the RNAP purified from exponential phase shows low promoter specificity in promoter-polymerase interaction studies due to the presence of a large number of sigma factors during exponential phase and under-representation of sigma A required for house-keeping transcription
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additional information
?
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the RNAP purified from exponential phase shows low promoter specificity in promoter-polymerase interaction studies due to the presence of a large number of sigma factors during exponential phase and under-representation of sigma A required for house-keeping transcription
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additional information
?
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the two rpoB paralogues, rpoB(S) and rpoB(R), are two functionally distinct and developmentally regulated RNA polymerases, overview. A five amino acid substitutions located within or close to the so-called rifampin resistance clusters of rpoB(R) plays a key role in fundamental activities of the RNA polymerase. The rpoB(R)-specific missense mutation H426N is essential for the activation of secondary metabolism, molecular mechanism, overview
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?
additional information
?
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identification of an activity associated with the mtRNAP in which non-DNA-templated nucleotides are added to the 3' end of RNAs, any of the four rNTPs can act as precursors for this process, RNA editing mechanism, overview. Nucleotides that are not specified by the mitochondrial DNA templates are inserted into some RNAs, a process called RNA editing. This is an essential step in the expression of these RNAs, as the insertion of the nontemplated nucleotides creates open reading frames for the production of proteins from mRNAs or produces required secondary structure in rRNAs and tRNAs
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additional information
?
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bacterial anti-sigma factors typically regulate sigma factor function by restricting the access of their cognate sigma-factors to the RNA polymerase RNAP core enzyme, regulation of RNAP holoenzyme, Esigma70, involving Rsd and the Rsd orthologue AlgQ, a global regulator of gene expression in Pseudomonas aeruginosa, which simultaneously interact with conserved region 2 and region 4 of sigma70 mediated by separate surfaces of Rsd, interaction with mutants of Rsd and AlgQ, mechanism, detailed overview. Rsd can strongly regulate the production of the Pseudomonas aeruginosa virulence factor pyocyanin in a manner that depends on their abilities to interact with sigma70 region 2
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?
additional information
?
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molecular mechanisms enabling sigma factor PvdS, directing the transcription of pyoverdine and virulence genes under iron limitation, to compete with the major sigma RpoD for RNA polymerase binding, overview
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?
additional information
?
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multi-subunit DNA-dependent RNA polymerases synthesize RNA molecules thousands of nucleotides long. The reiterative reaction of nucleotide condensation occurs at rates of tens of nucleotides per second, invariably linked to the translocation of the enzyme along the DNA template, or threading of the DNA and the nascent RNA molecule through the enzyme. Reiteration of the nucleotide addition/translocation cycle without dissociation from the DNA and RNA requires both isomorphic and metamorphic conformational flexibility of a magnitude substantial enough to accommodate the requisite molecular motions
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?
additional information
?
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RNAP function through the transcription cycle with initiation/re-initiation, elongation, and termination, detailed overview
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?
additional information
?
-
-
RNAP adds nucleotides to the 3'-end of the growing RNA and translocates reiteratively, in single nucleotide steps. Translocation mechanism models, concerning conformational changes, allosteric effects and isomerization, and model evaluation, overview
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-
?
additional information
?
-
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the enzyme active site is located on the back wall of the channel, where an essential Mg2+ ion is chelated by three Asp of the absolutely conserved NADFDGD motif in the A' subunit
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?
additional information
?
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multi-subunit DNA-dependent RNA polymerases synthesize RNA molecules thousands of nucleotides long. The reiterative reaction of nucleotide condensation occurs at rates of tens of nucleotides per second, invariably linked to the translocation of the enzyme along the DNA template, or threading of the DNA and the nascent RNA molecule through the enzyme. Reiteration of the nucleotide addition/translocation cycle without dissociation from the DNA and RNA requires both isomorphic and metamorphic conformational flexibility of a magnitude substantial enough to accommodate the requisite molecular motions
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?
additional information
?
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peptide regions that interact with regulatory factors are close to the Pol II surface and assume seemingly flexible loop structures, one is located in the TFIIF-interacting protrusion domain, the other is located in the TFIIE-interacting clamp domain, conformations, overview
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?
additional information
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RNAP function through the transcription cycle with initiation/re-initiation, elongation, and termination, detailed overview
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additional information
?
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RNAPII recruits COMPASS, a histone methyltransferase, as well as the regulator Paf1C, to the transcription active site causing methylation of histone H3K4 in a transcription-dependent manner. The large RNAPII subunit Rpb1 attracts FACT, a transcription factor that FACT participates in regulation of DNA repair and replication, to the transcription site, and Rpb1 also interacts with RSC, an abundant Swi/Snf-like chromatin remodeling complex with multiple subunits, and other general transcription factors, as well as with histone chaperone proteins, mRNA processing and export factors, DNA repair factors, protein kinases, and other cellular proteins, overview
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additional information
?
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the phosphatase activity of Cdc14 is required for Pol I inhibition, transcription inhibition is necessary for complete chromosome disjunction, because rRNA transcripts block condensin binding to rDNA, and show that bypassing the role of Cdc14 in nucleolar segregation requires in vivo degradation of nascent transcripts, transcription interferes with chromosome condensation, not the reverse
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additional information
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the Switch 1 loop of RNA polymerase II, located at the downstream end of the transcription bubble, may operate as a specific sensor of the nucleoside triphosphates available for transcription. Regulatory effects of RNA polymerase II on URA2 gene, encoding the rate-limiting enzyme of UTP biosynthesis after activation by UTP shortage, RNA polymerase II occupancy is increased on the URA2 open reading frame, overview
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additional information
?
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RNAP adds nucleotides to the 3'-end of the growing RNA and translocates reiteratively, in single nucleotide steps. Translocation mechanism models, concerning conformational changes, allosteric effects and isomerization, and model evaluation, overview
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?
additional information
?
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the enzyme also shows RNA-dependent RNA polymerase activity, EC 2.7.7.48, but slower and less processive than the DNA-dependent activity. During active transcription, Pol II must overcome intrinsic DNA-arrest sites, which are generally rich in A-T base pairs and pose a natural obstacle to transcription. At such sites, Pol II moves backwards along DNA and RNA, resulting in extrusion of the RNA 3' end through the polymerase pore beneath the active site and transcriptional arrest. The RNA cleavage stimulatory factor TFIIS can rescue an arrested polymerase by creating a new RNA 3' end at the active site from which transcription can resume, mechanism, overview
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additional information
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mitochondrial RNA polymerase (Rpo41) and its transcription factor (Mtf1) are an efficient primase that initiates DNA synthesis on ssDNA coated with the yeast mitochondrial ssDNA-binding protein, Rim1. Both Rpo41 and Rpo41-Mtf1 can synthesize short and long RNAs on ssDNA template and prime DNA synthesis by the yeast mitochondrial DNA polymerase Mip1. Regarding the RNA-DNA products, Rpo41 and Rpo41-Mtf1 have slightly different priming specificity. Both prefer to initiate with ATP from short priming sequences such as 3'-TCC, TTC, and TTT, and the consensus sequence is 3'-Pu(Py)2-3
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additional information
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quantitative reverse transcriptase-PCR expression analysis
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additional information
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quantitative reverse transcriptase-PCR expression analysis
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additional information
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determination of the substrate binding site
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?
additional information
?
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multi-subunit DNA-dependent RNA polymerases synthesize RNA molecules thousands of nucleotides long. The reiterative reaction of nucleotide condensation occurs at rates of tens of nucleotides per second, invariably linked to the translocation of the enzyme along the DNA template, or threading of the DNA and the nascent RNA molecule through the enzyme. Reiteration of the nucleotide addition/translocation cycle without dissociation from the DNA and RNA requires both isomorphic and metamorphic conformational flexibility of a magnitude substantial enough to accommodate the requisite molecular motions
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?
additional information
?
-
-
RNAP function through the transcription cycle with initiation/re-initiation, elongation, and termination, detailed overview
-
-
?
additional information
?
-
-
RNAP adds nucleotides to the 3'-end of the growing RNA and translocates reiteratively, in single nucleotide steps. Translocation mechanism models, concerning conformational changes, allosteric effects and isomerization, and model evaluation, overview
-
-
?
additional information
?
-
-
multi-subunit DNA-dependent RNA polymerases synthesize RNA molecules thousands of nucleotides long. The reiterative reaction of nucleotide condensation occurs at rates of tens of nucleotides per second, invariably linked to the translocation of the enzyme along the DNA template, or threading of the DNA and the nascent RNA molecule through the enzyme. Reiteration of the nucleotide addition/translocation cycle without dissociation from the DNA and RNA requires both isomorphic and metamorphic conformational flexibility of a magnitude substantial enough to accommodate the requisite molecular motions
-
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?
additional information
?
-
-
RNAP adds nucleotides to the 3'-end of the growing RNA and translocates reiteratively, in single nucleotide steps. Translocation mechanism models, concerning conformational changes, allosteric effects and isomerization, and model evaluation, overview
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?
additional information
?
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the RNAP clamp head domain constitutes the wall of the main channel opposite the catalytic centre and forms crucial contacts with the DNA template strand in the elongation complex
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additional information
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the PSi-C-terminal domain of large subunit RPB1 is essential for cell survivial and production of both SL RNA and mRNA, the Trypanosoma brucei enzyme lacks conserved heptapeptide sequence motifs found in most other eukaryotes
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additional information
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in vitro transcriptional activity of recombinant assembled Xcc RNAP, overview
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additional information
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in vitro transcriptional activity of recombinant assembled Xcc RNAP, overview
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additional information
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in vitro transcriptional activity of recombinant assembled Xcc RNAP, overview
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additional information
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in vitro transcriptional activity of recombinant assembled Xcc RNAP, overview
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + RNAn
diphosphate + RNAn+1
CTP + RNAn
diphosphate + RNAn+1
GTP + RNAn
diphosphate + RNAn+1
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
additional information
?
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ATP + RNAn
diphosphate + RNAn+1
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ATP + RNAn
diphosphate + RNAn+1
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ATP + RNAn
diphosphate + RNAn+1
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ATP + RNAn
diphosphate + RNAn+1
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CTP + RNAn
diphosphate + RNAn+1
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CTP + RNAn
diphosphate + RNAn+1
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GTP + RNAn
diphosphate + RNAn+1
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GTP + RNAn
diphosphate + RNAn+1
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nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
Autographa californica M nucleopolyhedrovirus transcribes genes using two DNA-directed RNA polymerases. Early genes are transcribed by the host RNA polymerase II, and late and very late genes are transcribed by a viral-encoded multisubunit RNA polymerase
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nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
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?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
RNAP is an exceptionally complex enzyme that can be thought of as the engine of gene expression, synthesis of RNA transcripts of many thousands of nucleotides without dissociation. Energy, in the form of nucleoside triphosphates, fuels the synthesis of an RNA polymer complementary to specific regions of the DNA template. Like all macromolecular synthesis, RNA synthesis can be divided into three general phases: initiation, elongation, and termination. Importantly, each of these phases can be a target of regulation. Promoter recognition, binding at the extended promoter recognition region, and transcript initiation, RNAP prefers to initiate transcription within a narrow window located between 6 and 9 bp downstream of the -10 element, promoter clearance and elongation, termination and recycling, mechanisms and regulation , overview. The process of start site selection can be governed by the availability of either the +1 or the +2 NTP, depending on the promoter
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nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
transcription elongation as a critical regulatory step in addition to initiation
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nucleoside triphosphate + RNAn
diphosphate + RNAn+1
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nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
template is DNA
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?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
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nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
a kind of transcription complex is formed during RNA polymerase catalysed synthesis of the M13 bacteriophage replication primer. The complex contains an overextended RNADNA hybrid bound in the RNA-polymerase through that is normally occupied by downstream double-stranded DNA, thus leaving the 30 end of the RNA available for interaction with DNA polymerase
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?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
enzyme is responsible for transcription in bacteria
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?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
regulation by anions, overview
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?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
RNAP is an exceptionally complex enzyme that can be thought of as the engine of gene expression, synthesis of RNA transcripts of many thousands of nucleotides without dissociation. Energy, in the form of nucleoside triphosphates, fuels the synthesis of an RNA polymer complementary to specific regions of the DNA template. Like all macromolecular synthesis, RNA synthesis can be divided into three general phases: initiation, elongation, and termination. Importantly, each of these phases can be a target of regulation. Promoter recognition, binding at the extended promoter recognition region, and transcript initiation, RNAP prefers to initiate transcription within a narrow window located between 6 and 9 bp downstream of the -10 element, promoter clearance and elongation, termination and recycling, mechanisms and regulation , overview. The process of start site selection can be governed by the availability of either the +1 or the +2 NTP, depending on the promoter
-
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?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
template is DNA
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?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
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?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
mediates fast promoter-independent extension of unstable nucleic acid complexes
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?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the single subunit DNA-dependent RNA polymerase from bacteriophage T7 catalyzes both promoterdependent transcription initiation and promoter-independent elongation
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?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
template is DNA
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?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
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?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the hepatitis delta virus is an RNA virus that depends on DNA-dependent RNA polymerase for its transcription and replication. The association between human RNAP II and hepatitis delta virus RNA suggest two transcription start sites on both polarities of hepatitis delta virus RNA
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nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
RNAPIIis recruited to gene promoters in a hypo-phosphorylated state
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?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
template is DNA, epigenetic control of rDNA transcription, regulation system of RNA polymerase, detailed overview
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nucleoside triphosphate + RNAn
diphosphate + RNAn+1
Inovirus M13
-
minimal M13 origin hairpin is bound in the RNAP core channel normally occupied by dsDNA downstream of the transcription initiation start site, the sigma subunit is not required for initiation of RNA synthesis but it is essential for escape into productive elongation, RNAP recognition of the M13 ori and mechanism of RNA synthesis during transcription, detailed overview. During transcription elongation, RNAP can processively synthesize RNAs for thousands of nt. Mechanism of priming on dsDNA, overview
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?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
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?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
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template is DNA, epigenetic control of rDNA transcription, regulation system of RNA polymerase, detailed overview
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?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
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nucleoside triphosphate + RNAn
diphosphate + RNAn+1
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?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
recruitment of the enzyme is a rate-limiting step for the activation of the sigma(54) promoter Pu of Pseudomonas putida, overview
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nucleoside triphosphate + RNAn
diphosphate + RNAn+1
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nucleoside triphosphate + RNAn
diphosphate + RNAn+1
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?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
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?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
template is DNA
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?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
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nucleoside triphosphate + RNAn
diphosphate + RNAn+1
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nucleoside triphosphate + RNAn
diphosphate + RNAn+1
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nucleoside triphosphate + RNAn
diphosphate + RNAn+1
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the enzyme can bind to DNA containing the lambdaPR promoter, form an open complex and initiate transcription in a temperature-dependent manner. The organism relies on the high temperature of its environment to provide the thermal energy required to stimulate open promoter complex formation, initiate transcription, and facilitate the conformational changes in RNA polymerase that results in nucleotide incorporation
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?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme can bind to DNA containing the lambdaPR promoter, form an open complex and initiate transcription in a temperature-dependent manner. The organism relies on the high temperature of its environment to provide the thermal energy required to stimulate open promoter complex formation, initiate transcription, and facilitate the conformational changes in RNA polymerase that results in nucleotide incorporation
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?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
nucleoside triphosphate phosphohydrolase I binds to the H4L subunit of virion RNA polymerase. These observation provides an explanation that UUUUUNU-dependent transcription termination is restricted to early genes, whose transcription is catalyzed by the H4L-containing virion RNA polymerase
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?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
nucleoside triphosphate phosphohydrolase I binds to the H4L subunit of virion RNA polymerase. These observation provides an explanation that UUUUUNU-dependent transcription termination is restricted to early genes, whose transcription is catalyzed by the H4L-containing virion RNA polymerase
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?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
Zindervirus SP6
-
template is DNA
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?
additional information
?
-
-
multi-subunit DNA-dependent RNA polymerases synthesize RNA molecules thousands of nucleotides long. The reiterative reaction of nucleotide condensation occurs at rates of tens of nucleotides per second, invariably linked to the translocation of the enzyme along the DNA template, or threading of the DNA and the nascent RNA molecule through the enzyme. Reiteration of the nucleotide addition/translocation cycle without dissociation from the DNA and RNA requires both isomorphic and metamorphic conformational flexibility of a magnitude substantial enough to accommodate the requisite molecular motions
-
-
?
additional information
?
-
-
RNA polymerase binds multiple sites in the ehxCABD gene regulatory region. At the Escherichia coli ehxCABD operon, RNA polymerase is unable to distinguish between the promoter -10 element and similar overlapping sequences. RNA polymerase competes with itself for binding to AT-rich sequences overlapping PehxCABD, correct positioning of RNA polymerase at PehxCABD requires H-NS
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?
additional information
?
-
-
molecular mechanisms of transcription regulation in mitochondria, molecular organization of the human mitochondrial transcription initiation complex, overview
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?
additional information
?
-
-
RNA pol III transcribes structural RNAs involved in RNA processing, U6 snRNA, and translation, tRNA. Mechanism of regulation of RNA pol III transcription by BRCA1, overview
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-
?
additional information
?
-
-
RNA polymerase II phosphorylation during paused, active and poised transcription cycles with in itiation and elongation stages and at different phosphorylation stages, RNA polymerase II and histone modification profiles across genes in paused, active and poised states, and RNAPII regulation mechanisms at active genes, detailed overview. In embryonic stem cells, silent developmental regulator genes that are repressed by Polycomb are associated with a form of RNAPII that can elongate through coding regions but that lacks the post-translational modifications that are important for coupling RNA synthesis to co-transcriptional maturation
-
-
?
additional information
?
-
-
TLS regulates both RNAPs II and III and supports the possibility that cross-regulation between RNA polymerases is important in maintaining normal cell growth
-
-
?
additional information
?
-
-
two distinct forms, Pol Ialpha and Pol Ibeta. Both forms are catalytically active, but only Pol Ibeta can assemble into productive transcription initiation complexes. Regulation of Pol I transcription during cell cycle progression involving cytokines, and structural organization of mammalian rDNA repeats and the basal factors required for transcription initiation, overview. The activity of basal Pol I factors is regulated by posttranslational modifications
-
-
?
additional information
?
-
-
RNA polymerase III transcribes small untranslated RNAs that include tRNAs, 5S RNA, U6 RNA, and some microRNAs
-
-
?
additional information
?
-
-
the B2 family of short interspersed elements is transcribed into non-coding RNA by RNA polymerase III
-
-
?
additional information
?
-
Inovirus M13
-
multisubunit RNA polymerase transcribes DNA, but is also known to synthesize DNA replication primers in the replication system, a function that is commonly performed by primases, mechanism of primer synthesis by RNA polymerase and comparison to the mechanism of both types of primases, overview
-
-
?
additional information
?
-
-
RNAP II participates in the generation of mRNAs and most of the small nuclear RNAs, while RNAP III synthesizes small essential RNAs, such as tRNAs, 5S rRNA and some snRNAs
-
-
?
additional information
?
-
-
RNAP II participates in the generation of mRNAs and most of the small nuclear RNAs, while RNAP III synthesizes small essential RNAs, such as tRNAs, 5S rRNA and some snRNAs
-
-
?
additional information
?
-
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intermittent hypoxia, a major pathological factor in the development of neural deficits associated with sleep-disordered breathing, regulates RNA polymerase II in hippocampus and prefrontal cortex. Chronic intermittent hypoxia, but not sustained hypoxia, stimulates hydroxylation of Pro1465 in large subunit of RNA polymerase II and phosphorylation of Ser5 of Rpb1, specifically in the CA1 region of the hippocampus and in the prefrontal cortex but not in other regions of the brain, requiring the von Hippel-Lindau tumor suppressor. Mice exposed to chronic IH demonstrated cognitive deficits related to dysfunction in those brain regions, overview
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?
additional information
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two distinct forms, Pol Ialpha and Pol Ibeta. Both forms are catalytically active, but only Pol Ibeta can assemble into productive transcription initiation complexes. Regulation of Pol I transcription during cell cycle progression involving cytokines, and structural organization of mammalian rDNA repeats and the basal factors required for transcription initiation, overview. The activity of basal Pol I factors is regulated by posttranslational modifications
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additional information
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the enzyme binds to the iNOS promoter
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additional information
?
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the two rpoB paralogues, rpoB(S) and rpoB(R), are two functionally distinct and developmentally regulated RNA polymerases, overview. A five amino acid substitutions located within or close to the so-called rifampin resistance clusters of rpoB(R) plays a key role in fundamental activities of the RNA polymerase. The rpoB(R)-specific missense mutation H426N is essential for the activation of secondary metabolism, molecular mechanism, overview
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?
additional information
?
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bacterial anti-sigma factors typically regulate sigma factor function by restricting the access of their cognate sigma-factors to the RNA polymerase RNAP core enzyme, regulation of RNAP holoenzyme, Esigma70, involving Rsd and the Rsd orthologue AlgQ, a global regulator of gene expression in Pseudomonas aeruginosa, which simultaneously interact with conserved region 2 and region 4 of sigma70 mediated by separate surfaces of Rsd, interaction with mutants of Rsd and AlgQ, mechanism, detailed overview. Rsd can strongly regulate the production of the Pseudomonas aeruginosa virulence factor pyocyanin in a manner that depends on their abilities to interact with sigma70 region 2
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additional information
?
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molecular mechanisms enabling sigma factor PvdS, directing the transcription of pyoverdine and virulence genes under iron limitation, to compete with the major sigma RpoD for RNA polymerase binding, overview
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additional information
?
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multi-subunit DNA-dependent RNA polymerases synthesize RNA molecules thousands of nucleotides long. The reiterative reaction of nucleotide condensation occurs at rates of tens of nucleotides per second, invariably linked to the translocation of the enzyme along the DNA template, or threading of the DNA and the nascent RNA molecule through the enzyme. Reiteration of the nucleotide addition/translocation cycle without dissociation from the DNA and RNA requires both isomorphic and metamorphic conformational flexibility of a magnitude substantial enough to accommodate the requisite molecular motions
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additional information
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RNAP function through the transcription cycle with initiation/re-initiation, elongation, and termination, detailed overview
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additional information
?
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multi-subunit DNA-dependent RNA polymerases synthesize RNA molecules thousands of nucleotides long. The reiterative reaction of nucleotide condensation occurs at rates of tens of nucleotides per second, invariably linked to the translocation of the enzyme along the DNA template, or threading of the DNA and the nascent RNA molecule through the enzyme. Reiteration of the nucleotide addition/translocation cycle without dissociation from the DNA and RNA requires both isomorphic and metamorphic conformational flexibility of a magnitude substantial enough to accommodate the requisite molecular motions
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?
additional information
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peptide regions that interact with regulatory factors are close to the Pol II surface and assume seemingly flexible loop structures, one is located in the TFIIF-interacting protrusion domain, the other is located in the TFIIE-interacting clamp domain, conformations, overview
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additional information
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RNAP function through the transcription cycle with initiation/re-initiation, elongation, and termination, detailed overview
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additional information
?
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RNAPII recruits COMPASS, a histone methyltransferase, as well as the regulator Paf1C, to the transcription active site causing methylation of histone H3K4 in a transcription-dependent manner. The large RNAPII subunit Rpb1 attracts FACT, a transcription factor that FACT participates in regulation of DNA repair and replication, to the transcription site, and Rpb1 also interacts with RSC, an abundant Swi/Snf-like chromatin remodeling complex with multiple subunits, and other general transcription factors, as well as with histone chaperone proteins, mRNA processing and export factors, DNA repair factors, protein kinases, and other cellular proteins, overview
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?
additional information
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the phosphatase activity of Cdc14 is required for Pol I inhibition, transcription inhibition is necessary for complete chromosome disjunction, because rRNA transcripts block condensin binding to rDNA, and show that bypassing the role of Cdc14 in nucleolar segregation requires in vivo degradation of nascent transcripts, transcription interferes with chromosome condensation, not the reverse
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additional information
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the Switch 1 loop of RNA polymerase II, located at the downstream end of the transcription bubble, may operate as a specific sensor of the nucleoside triphosphates available for transcription. Regulatory effects of RNA polymerase II on URA2 gene, encoding the rate-limiting enzyme of UTP biosynthesis after activation by UTP shortage, RNA polymerase II occupancy is increased on the URA2 open reading frame, overview
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additional information
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mitochondrial RNA polymerase (Rpo41) and its transcription factor (Mtf1) are an efficient primase that initiates DNA synthesis on ssDNA coated with the yeast mitochondrial ssDNA-binding protein, Rim1. Both Rpo41 and Rpo41-Mtf1 can synthesize short and long RNAs on ssDNA template and prime DNA synthesis by the yeast mitochondrial DNA polymerase Mip1. Regarding the RNA-DNA products, Rpo41 and Rpo41-Mtf1 have slightly different priming specificity. Both prefer to initiate with ATP from short priming sequences such as 3'-TCC, TTC, and TTT, and the consensus sequence is 3'-Pu(Py)2-3
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additional information
?
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multi-subunit DNA-dependent RNA polymerases synthesize RNA molecules thousands of nucleotides long. The reiterative reaction of nucleotide condensation occurs at rates of tens of nucleotides per second, invariably linked to the translocation of the enzyme along the DNA template, or threading of the DNA and the nascent RNA molecule through the enzyme. Reiteration of the nucleotide addition/translocation cycle without dissociation from the DNA and RNA requires both isomorphic and metamorphic conformational flexibility of a magnitude substantial enough to accommodate the requisite molecular motions
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?
additional information
?
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RNAP function through the transcription cycle with initiation/re-initiation, elongation, and termination, detailed overview
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?
additional information
?
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-
multi-subunit DNA-dependent RNA polymerases synthesize RNA molecules thousands of nucleotides long. The reiterative reaction of nucleotide condensation occurs at rates of tens of nucleotides per second, invariably linked to the translocation of the enzyme along the DNA template, or threading of the DNA and the nascent RNA molecule through the enzyme. Reiteration of the nucleotide addition/translocation cycle without dissociation from the DNA and RNA requires both isomorphic and metamorphic conformational flexibility of a magnitude substantial enough to accommodate the requisite molecular motions
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?
additional information
?
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the PSi-C-terminal domain of large subunit RPB1 is essential for cell survivial and production of both SL RNA and mRNA, the Trypanosoma brucei enzyme lacks conserved heptapeptide sequence motifs found in most other eukaryotes
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(S)-2-((1-amino-1-oxo-3-phenylpropan-2-ylamino)methyl)-3-(4-amino phenoxy)-5-methoxy phenyl acetate
(S)-2-((1-amino-1-oxo-3-phenylpropan-2-ylamino)methyl)-5-methoxy-3-(4-nitrophenoxy)phenyl acetate
(S)-2-((1-amino-3-(4-hydroxyphenyl)-1-oxopropan-2-ylamino)methyl)-3-(4-aminophenoxy)-5-methoxyphenyl acetate
(S)-2-((1-amino-3-(4-hydroxyphenyl)-1-oxopropan-2-ylamino)methyl)-5-methoxy-3-(4-nitrophenoxy)phenyl acetate
1,3-dimethoxy-5-(4-nitrophenoxy) benzene
1-(3-C-ethynyl-beta-D-ribo-pentofuranosyl)cytosine
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i.e. ECyd, TAS-106, a antitumor ribonucleoside that inhibits RNA polymerase, acts synergistically in inhibiting A-549 cancer cell growth and in tumor growth in vivo. The compound also inhibits the checkpoint-associated protein, the expression of Chk1 protein and the phosphorylation of Chk1 and Chk2, antitumour effects in combination with cisplatin, overview
1-[2-[3-(4-Chloro-3-trifluoromethylphenyl)ureido]-4-trifluoromethyl phenoxy]-4,5-dichlorobenzene sulfonic acid
-
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2'-C-ethynyl-7-deaza-ATP
causes immediate chain termination
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2'-C-Me-ATP
causes immediate chain termination
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2,4-dimethoxy-6-(4-nitrophenoxy) benzaldehyde
2-([[(1S)-2-amino-1-(4-hydroxybenzyl)-2-oxoethyl]amino]methyl)-5-methoxy-3-(4-nitrophenoxy)phenyl acetate
2-acetyl-3-hydroxy-5-methoxyphenyl acetate
2-acetyl-5-methoxy-3-(4-nitrophenoxy)phenyl acetate
2-formyl-5-methoxy-3-(4-nitrophenoxy)phenyl acetate
2-hydroxy-4-methoxy-6-(4-nitrophenoxy) benzaldehyde
3'-dATP
causes immediate chain termination
3'-ethynylcytidine-5'-triphosphate
-
i.e. ECTP, competitive inhibition in the presence of isolated nuclei from FM3A mouse tumor cells
4-[2-([[(1S)-2-amino-1-(4-hydroxybenzyl)ethyl]amino]methyl)-5-methoxy-3-(2-oxopropyl)benzyl]benzaldehyde
6,10,6'-tri-O-tert-butyldimethylsilyl-6-epi-catalpol
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ara-ATP
causes partial chain termination
B2 RNA
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the about 180-nt B2 RNA potently represses mRNA transcription by binding tightly to RNA polymerase II and assembling with it into complexes on promoter DNA, where it keeps the polymerase from properly engaging the promoter DNA. The C-terminal domain of the largest Pol II subunit is not involved. B2 RNA binds Pol II and assembles into complexes at promoters. Binding site anaylsis usig Pol II peptides, binding structure, and mechanism of transcriptional repression by B2 RNA, detailed overview
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breast cancer susceptibility gene 1
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BRCA1, inhibits RNA pol III via inhibition of the essential transcription factor TFIIIB, mechanism, overview. BRCA1 is a tumor suppressor playing a role in DNA repair, cell cycle regulation, apoptosis, genome integrity, and ubiquitination, and it BRCA1 has a conserved N-terminal RING domain, an activation domain 1, AD1, and an acidic C-terminal domain, BRCA1 C-terminal region. Interaction with TFIIIB occurs via the BRCA1 C-terminal region domain of Fcp1p, an RNA polymerase II phosphatase. RNA pol III inhibition involves the TFIIB family members Brf1 and Brf2, overview
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CBR703
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the IC50s values are significantly decreased with template Kool NC-45, or increased with template poly(dA-dT)
Cdc14
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a protein phosphatase required for nucleolar segregation and mitotic exit4, inhibits RNA polymerase I, the phosphatase activity of Cdc14 is required for Pol I inhibition in vitro and in vivo involving nucleolar exclusion of Pol I subunits
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corallopyronin
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inhibition is not affected by template Kool NC-45
Cordycepin triphosphate
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d(Ap4C)
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d(Ap4T), d(Ap4C) and d(Ap4G) inhibit the incorporation of dATP into DNA less effectively than d(Ap4T), d(Tp4T) and d(Tp4C) the dTTP incorporation
d(Ap4G)
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d(Ap4T), d(Ap4C) and d(Ap4G) inhibit the incorporation of dATP into DNA less effectively than d(Ap4T), d(Tp4T) and d(Tp4C) the dTTP incorporation
d(Ap4T)
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d(Ap4T), d(Ap4C) and d(Ap4G) inhibit the incorporation of dATP into DNA less effectively than d(Ap4T), d(Tp4T) and d(Tp4C) the dTTP incorporation
d(Tp4C)
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d(Ap4T), d(Ap4C) and d(Ap4G) inhibit the incorporation of dATP into DNA less effectively than d(Ap4T), d(Tp4T) and d(Tp4C) the dTTP incorporation
d(Tp4T)
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d(Ap4T), d(Ap4C) and d(Ap4G) inhibit the incorporation of dATP into DNA less effectively than d(Ap4T), d(Tp4T) and d(Tp4C) the dTTP incorporation
DNA
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various DNA lesions significantly affect the efficiency and fidelity of RNA synthesis. DNA modifications that disrupt correct base-pairing can strongly inhibit transcription and increase nucleotide misincorporation by RNAP. The universal transcription factor GreA and Deinococcus-specific factor Gfh1 stimulate RNAP stalling at various DNA lesions, depending on the type of the lesion and the presence of Mn2+ ions
etoposide
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treatment with 0.02 mM etoposide leads to a transient inhibition of rRNA synthesis
Exotoxin of Bacillus thuringiensis
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ML-60218
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treatment of A-549 cells with the Pol III inhibitor ML-60218 decreased the cytosolic RNA:DNA hybrid staining
MnCl2
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in presence of 10 mM MgCl2
oxygen
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the enzyme is highly oxygen sensitive. Inactivation is accompanied by cross-linking of components. Inactivated enzyme can be reactivated by reduction with sodium dithionite
per-O-acetyl-verbascoside
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compound isolated from aerial part of Buddleja cordobensis Grisebach, most active among the compounds tested
procyclin-associated genes
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i.e. PAG1, PAG2 or PAG3, inhibit RNA synthesis, deletion of PAGs lead to increased mRNA levels, regulation of PAG expressions, overview
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protein Rim1
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the ssDNA-binding protein Rim1 severely inhibits theRNAsynthesis activity of Rpo41, but not the Rpo41-Mtf1 complex, which continues to prime DNA synthesis efficiently in the presence of Rim1
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protein TLS
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translocated in liposarcoma, a protein originally identified as the product of a chromosomal translocation, which associates with both RNAP II and the spliceosome, also represses transcription by RNAP III. It represses transcription from all three classes of RNAP III promoters in vitro and to associates with RNAP III genes in vivo. Depletion of TLS by siRNA in HeLa cells resulted in increased steady-state levels of RNAP III transcripts as well as increased RNAP III and TBP occupancy at RNAP III-transcribed genes
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RBL-1
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oligonucleotide, efficiently inhibits
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RECQL5
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a DNA helicase of the RECQ family, directly inhibits RNA polymerase II. It RECQL5 inhibits both initiation and elongation in transcription assays reconstituted with highly purified general transcription factors and RNAPII, RECQL5 helicase activity is not required for inhibition
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Spt5
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the large subunit of the DRB sensitivity-inducing factor, DSIF, represses or activates RNAPII elongation in vitro. CTR1 and CTR2CT, the two repeat-containing regions constituting the C-terminus of Spt5, play a redundant role in repressing RNAPII elongation in vivo, overview. Mutant NSpt5, lacking the C-terminus, directly associates with hsp70-4 chromatin in vivo and increases the occupancy of RNAPII, positive transcription elongation factor b, histone H3 Lys 4 trimethylation, and surprisingly, the negative elongation factor A at the locus, indicating a direct action of NSpt5 on the elongation repressed locus, nuclear extracts containing the constitutively active P-TEFb and WT DSIF lead to a time-dependent increase of the long, promoter-distal RNase T1-resistant products, reflecting the elongation stimulatory activity of Spt5, overview
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terminatin factor NsiI
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N-terminally FLAG-tagged fusion protein Nsi1 expressed from Sf21 insect cells. Binding of the termination factor Nsi1 to its cognate DNA site is sufficient to terminate RNA polymerase I transcription in vitro and to induce termination in vivo. Nsi1 contains Myb-like DNA binding domains and associates in vivo near the 3' end of rRNA genes to rDNA. Binding of Nsi1 to a stretch of 11 nucleotides in the correct orientation is sufficient to pause elongating Pol I shortly upstream of the Nsi1 binding site and to release the transcripts in vitro, and the same minimal DNA element triggers Nsi1-dependent termination of pre-rRNA synthesis in vivo. Termination efficiency in the in vivo system can be enhanced by inclusion of specific DNA sequences downstream of the Nsi1 binding site
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TFAM
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DNA packaging by TFAM makes the DNA more resistant to unwinding
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(S)-2-((1-amino-1-oxo-3-phenylpropan-2-ylamino)methyl)-3-(4-amino phenoxy)-5-methoxy phenyl acetate
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(S)-2-((1-amino-1-oxo-3-phenylpropan-2-ylamino)methyl)-3-(4-amino phenoxy)-5-methoxy phenyl acetate
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(S)-2-((1-amino-1-oxo-3-phenylpropan-2-ylamino)methyl)-5-methoxy-3-(4-nitrophenoxy)phenyl acetate
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(S)-2-((1-amino-1-oxo-3-phenylpropan-2-ylamino)methyl)-5-methoxy-3-(4-nitrophenoxy)phenyl acetate
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(S)-2-((1-amino-3-(4-hydroxyphenyl)-1-oxopropan-2-ylamino)methyl)-3-(4-aminophenoxy)-5-methoxyphenyl acetate
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(S)-2-((1-amino-3-(4-hydroxyphenyl)-1-oxopropan-2-ylamino)methyl)-3-(4-aminophenoxy)-5-methoxyphenyl acetate
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(S)-2-((1-amino-3-(4-hydroxyphenyl)-1-oxopropan-2-ylamino)methyl)-5-methoxy-3-(4-nitrophenoxy)phenyl acetate
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(S)-2-((1-amino-3-(4-hydroxyphenyl)-1-oxopropan-2-ylamino)methyl)-5-methoxy-3-(4-nitrophenoxy)phenyl acetate
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1,3-dimethoxy-5-(4-nitrophenoxy) benzene
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1,3-dimethoxy-5-(4-nitrophenoxy) benzene
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2,4-dimethoxy-6-(4-nitrophenoxy) benzaldehyde
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2,4-dimethoxy-6-(4-nitrophenoxy) benzaldehyde
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2-([[(1S)-2-amino-1-(4-hydroxybenzyl)-2-oxoethyl]amino]methyl)-5-methoxy-3-(4-nitrophenoxy)phenyl acetate
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2-([[(1S)-2-amino-1-(4-hydroxybenzyl)-2-oxoethyl]amino]methyl)-5-methoxy-3-(4-nitrophenoxy)phenyl acetate
-
-
2-acetyl-3-hydroxy-5-methoxyphenyl acetate
-
-
2-acetyl-3-hydroxy-5-methoxyphenyl acetate
-
-
2-acetyl-5-methoxy-3-(4-nitrophenoxy)phenyl acetate
-
-
2-acetyl-5-methoxy-3-(4-nitrophenoxy)phenyl acetate
-
-
2-formyl-5-methoxy-3-(4-nitrophenoxy)phenyl acetate
-
-
2-formyl-5-methoxy-3-(4-nitrophenoxy)phenyl acetate
-
-
2-hydroxy-4-methoxy-6-(4-nitrophenoxy) benzaldehyde
-
-
2-hydroxy-4-methoxy-6-(4-nitrophenoxy) benzaldehyde
-
-
4-[2-([[(1S)-2-amino-1-(4-hydroxybenzyl)ethyl]amino]methyl)-5-methoxy-3-(2-oxopropyl)benzyl]benzaldehyde
-
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4-[2-([[(1S)-2-amino-1-(4-hydroxybenzyl)ethyl]amino]methyl)-5-methoxy-3-(2-oxopropyl)benzyl]benzaldehyde
-
-
alpha-amanithin
-
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alpha-Amanitin
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alpha-amanitin inhibits Pol II by trapping the wedged trigger loop and shifted bridge helix, thereby stabilizing a conformation of the elongation complex that apparently represents a translocation intermediate
alpha-Amanitin
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the potent Sc RNAP II inhibitor binds to a ternary elongation complex with an open wedged conformation of the trigger loop
cisplatin
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a single cisplatin 1,2-d(CG) intrastrand cross-link or a single cisplatin 1,3-d(GTG) intrastrand cross-link is a strong block to the enzyme. The efficiency of the block at a cisplatin 1,2-d(GG) intrastrand cross-link is similar in several different nucleotide sequence contexts. Some blockage is also observed when the single cisplatin 1,3-d(GTG) intrastrand cross-link is located in the non-transcribed strand. Cisplatin-induced lesions in the transcribed DNA strand constitute a strong physical barrier to RNA polymerase progression
cisplatin
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a single cisplatin 1,2-d(CG) intrastrand cross-link or a single cisplatin 1,3-d(GTG) intrastrand cross-link is a strong block to the enzyme. The efficiency of the block at a cisplatin 1,2-d(GG) intrastrand cross-link is similar in several different nucleotide sequence contexts. Some blockage is also observed when the single cisplatin 1,3-d(GTG) intrastrand cross-link is located in the non-transcribed strand. Cisplatin-induced lesions in the transcribed DNA strand constitute a strong physical barrier to RNA polymerase progression
etnangien
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from the myxobacterium Sorangium cellulosum, a poly-unsaturated 22-membered polyketide macrolide, inhibits bacterial RNA polymerase, shows no cross-resistance to rifampicin
etnangien
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from the myxobacterium Sorangium cellulosum, a poly-unsaturated 22-membered polyketide macrolide, inhibits bacterial RNA polymerase, shows no cross-resistance to rifampicin, poor inhibition
etnangien
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from the myxobacterium Sorangium cellulosum, a poly-unsaturated 22-membered polyketide macrolide, inhibits bacterial RNA polymerase, shows no cross-resistance to rifampicin
etnangien
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from the myxobacterium Sorangium cellulosum, a poly-unsaturated 22-membered polyketide macrolide, inhibits bacterial RNA polymerase, shows no cross-resistance to rifampicin
etnangien
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from the myxobacterium Sorangium cellulosum, a poly-unsaturated 22-membered polyketide macrolide, inhibits bacterial RNA polymerase, shows no cross-resistance to rifampicin
etnangien
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from the myxobacterium Sorangium cellulosum, a poly-unsaturated 22-membered polyketide macrolide, inhibits bacterial RNA polymerase, poor inhibition of the yeast enzyme
etnangien
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from the myxobacterium Sorangium cellulosum, a poly-unsaturated 22-membered polyketide macrolide, inhibits bacterial RNA polymerase, shows no cross-resistance to rifampicin
etnangien methyl ester
-
-
etnangien methyl ester
-
weak inhibition
etnangien methyl ester
-
-
etnangien methyl ester
-
-
etnangien methyl ester
-
-
etnangien methyl ester
-
very weak inhibition
etnangien methyl ester
-
-
heparin
-
-
myxopyronin
-
an alpha-pyrone antibiotic, targets the RNAP switch region, which is the hinge that mediates opening and closing of the RNAP active-center cleft. Lower values for inhibition by myxopyronin in the presence of template Kool NC-45
myxopyronin
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produced by the bacteria Myxococcus fulvus, inhibits initiation of RNA polymerase transcription and binding complex structure. The compounds inhibits the enzyme also from rifamycin- or multidrug-resistant bacteria. the inhibition mechanism proceeds via inhibiting DNA binding rather than affecting transcription complex stability or processivity following DNA binding, overview
myxopyronin
-
inhibits bacterial RNA polymerase and inhibits transcription on the artificially melted promoters, inhibition mechanism, overview. The antibiotic binds to a pocket deep inside the RNAP clamp head domain, which interacts with the DNA template in the transcription bubble, binding of dMyx stabilizes refolding of the beta'-subunit switch-2 segment, resulting in a configuration that might indirectly compromise binding to, or directly clash with, the melted template DNA strand, binding structure, overview. Antibiotic binding does not prevent nucleation of the promoter DNA melting but instead blocks its propagation towards the active site. dMyx binds in the pocket deep inside the RNAP clamp head domain. Mutations designed in switch-2 mimic the dMyx effects on promoter complexes in the absence of antibiotic
protein gp76
-
the Thermus phage protein gp76 inhibits Escherichia coli RNAP highlighting the template-DNA binding site as a target site for developing antibacterial agents
-
protein gp76
the Thermus phage protein binds within the RNAP cleft and occupies the path of the template DNA strand at positions -11 to -4, relative to the transcription start site at +1. Thus, gp76 obstructs the formation of an open promoter complex and prevents transcription by Thermus thermophilus RNAP from most host promoters
-
rifampicin
-
0.1 mg/ml, complete inhibition
rifampicin
-
0.00006 mg/ml, 50% inactivation
sorangicin A
-
-
sorangicin A
inhibits the wild-type and mutant (S447/S456L) RNA polymerase through different mechanisms. It has a better pharmacokinetic profile than rifampicin, making it a suitable starting molecule to design drugs to be used for the treatment of tuberculosis patients with comorbidities who require multiple medications
sorangicin A
inhibits the wild-type and mutant (S447/S456L) RNA polymerase through different mechanisms. It has a better pharmacokinetic profile than rifampicin, making it a suitable starting molecule to design drugs to be used for the treatment of tuberculosis patients with comorbidities who require multiple medications; the inhibitor binds in the Rif-binding pocket of RNA. It inhibits inhibits the wild-type enzyme (RNAP) by a similar mechanism as rifampicin by preventing the translocation of very short RNAs. It inhibits the RifR S456L enzyme at an earlier step, preventing the transition of a partially unwound promoter DNA intermediate to the fully opened DNA and blocking the template-strand DNA from reaching the active site in the RNAP catalytic center
Streptolydigin
-
-
Streptolydigin
-
the antibiotic binds to a Tt RNAP TEC with an open trigger loop
Tagetitoxin
-
inhibition of RNA polymerase III
Tagetitoxin
-
no inhibition of calf thymus RNA polymerase II
Tagetitoxin
-
inhibition of RNA polymerase III
Tagetitoxin
-
50% inhibition at 0.0001 mM. Complete inhibition at 0.01 mM
Tagetitoxin
-
inhibition of RNA polymerase III
Tagetitoxin
-
inhibition of RNA polymerase III
additional information
-
synthesis of simplified etnangien analogues and analysis of their antimicrobial activities, overview
-
additional information
-
no inhibition by 0.1 mg/ml of rifampicin, streptolydigin or alpha-amanitin
-
additional information
-
despite relatively high overall sequence and structural homology between bacterial and mammalian core RNAP enzymes, there are sufficient differences between the enzyme classes for exploitation in the discovery of selective bacterial inhibitors
-
additional information
-
synthesis of simplified etnangien analogues and analysis of their antimicrobial activities, overview
-
additional information
-
the use of dsDNA templates containing classical promoters has only a negligible effects on the potency of enzyme inhibitors
-
additional information
-
FLiZ antagonize sigmaS-dependent gene expression in Escherichia coli. FliZ is an abundant DNA-binding protein and a global regulatory protein under the control of the flagellar master regulator FlhDC. It inhibits gene expression mediated by sigmaS by recognizing operator sequences that resemble the -10 region of sigmaS-dependent promoter. FLiZ plays a pivotal role in the decision between alternative life-styles, i.e. FlhDC-controlled flagellum-based motility or pS-dependent curli fimbriae-mediated adhesion and biofilm formation. FliZ is a global repressor with a DNA sequence specificity overlapping that of sigmaScontaining RNA polymerase, mechanism, overview
-
additional information
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no inhibition by epigallocatechin gallate
-
additional information
-
no inhibition by ent-16-ketobeyeran-19-oic acid, i.e. isosteviol, and related compounds
-
additional information
-
synthesis of simplified etnangien analogues and analysis of their antimicrobial activities, overview
-
additional information
-
inactivation of RNase P, by knockdown of RNase P subunits Rpp21, Rpp29 or Rpp38 by RNA interference, reduces the level of nascent transcription by Pol I, and more considerably that of Pol III, e.g. causing marked reduction in transcription of rDNA by Pol I
-
additional information
-
oncogenes and tumor suppressors control Pol I transcription, overview. Development of drugs that target the Pol I transcription machinery at different points, overveiw
-
additional information
-
Top1 inhibition favors Pol II escape from a promoter-proximal pausing site of the human HIF-1alpha gene in living cells. Top1 inhibition can trigger a transcriptional stress, involving antisense transcription and increased chromatin accessibility, which is dependent on cdk activity and deregulated Pol II pausing
-
additional information
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POLRMT is an off target for antiviral ribonucleoside analogues, unique mechanisms of mitochondrial transcription inhibition, overview
-
additional information
-
synthesis of simplified etnangien analogues and analysis of their antimicrobial activities, overview
-
additional information
-
gamma irradiation leads to a transient inhibition of rRNA synthesis, but Pol I transcription is not blocked by DNA damage itself, but by the action of DNA repair enzymes
-
additional information
-
oncogenes and tumor suppressors control Pol I transcription, overview. Development of drugs that target the Pol I transcription machinery at different points, overveiw
-
additional information
-
synthesis of simplified etnangien analogues and analysis of their antimicrobial activities, overview
-
additional information
-
no inhibition by NEM and iodoacetamide
-
additional information
-
no inhibition of RNA transcription by RECQL5 helicase-deficient point mutant RECQL5D157A, and another human RECQ family helicase, RECQL1
-
additional information
-
synthesis of simplified etnangien analogues and analysis of their antimicrobial activities, overview
-
additional information
-
a relatively short DNA region, lost in up2DELTA mutant and located immediately upstream of the URA2 initiator, impairs URA2 transcription by preventing RNA polymerase II from progressing towards the URA2open reading frame
-
additional information
-
synthesis of simplified etnangien analogues and analysis of their antimicrobial activities, overview
-
additional information
-
no inhibition by 0.1 mg/ml of rifampicin, streptolydigin or alpha-amanitin
-
additional information
-
no inhibition by 0.1 mg/ml of rifampicin, streptolydigin or alpha-amanitin
-
additional information
-
structure-based design of inhibitors with rifampicin as template, inhibitory potencies and binding mechanism via specific hydrogen-bonding sites involving residues Q390, F394, R405, Q567 and Q633, overview
-
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Ctk1
-
the kinase is required for the stability of the scaffold, but Ctk1 kinase activity is not required for the dissociation of basal transcription factors
-
glutamate
-
glutamate remodels the sigma38 transcription complex for activation. Accumulation of the simple signaling molecule glutamate can reprogram RNA polymerase in vitro without the need for specific protein receptors. During osmotic activation, glutamate appears to act as a Hofmeister series osmolyte to facilitate promoter escape. Escape is accompanied by a remodeling of the key interaction between the sigma38 stress protein and the beta-flap of the bacterial core RNA polymerase. This activation event contrasts with the established mechanism of inhibition in which glutamate, by virtue of its electrostatic properties, helps to inhibit binding to ribosomal promoters after osmotic shock
histone-like nucleoid structuring protein
-
i.e. H-NS, H-NS stimulates transcription from the F3 fragment, it can facilitate specific DNA-binding by RNA polymerase in AT-rich gene regulatory regions. Correct positioning of RNA polymerase at PehxCABD requires H-NS. Footprint of RNA polymerase (s70 RC461-FeBABE) interactions with -10 elements in the ehxCABD regulatory region in the presence of H-NS, overview
-
potassium acetate
-
activates
potassium aspartate
-
activates
potassium chloride
-
activates
potassium glutamate
-
activates highly, role of potassium ion in the activation of osmotic transcription
potassium nitrate
-
activates
RNase P
-
required for Pol I and Pol III required
-
sigma70
-
the sigma factor increases the transcription efficiency of templates with nonphysiological nonprokaryotic promoters
-
Spt5
-
the large subunit of the DRB sensitivity-inducing factor, DSIF, represses or activates RNAPII elongation in vitro. CTR1 and CTR2CT, the two repeat-containing regions constituting the C-terminus of Spt5, play a redundant role in repressing RNAPII elongation in vivo, overview. Mutant NSpt5, lacking the C-terminus, directly associates with hsp70-4 chromatin in vivo and increases the occupancy of RNAPII, positive transcription elongation factor b, histone H3 Lys 4 trimethylation, and surprisingly, the negative elongation factor A at the locus, indicating a direct action of NSpt5 on the elongation repressed locus, nuclear extracts containing the constitutively active P-TEFb and WT DSIF lead to a time-dependent increase of the long, promoter-distal RNase T1-resistant products, reflecting the elongation stimulatory activity of Spt5, overview
-
Spt6
-
transcription factor, Pol II shows a broad requirement for essential Spt6 during different stages of development, e.g. for for maximal recruitment of Paf1 and Spt5 to transcriptionally active Hsp70. Spt6 interacts with both nucleosome structure and Pol II, it has a role in elongation, directed RNAi knock-down of Spt6 reduces the elongation rate, the Spt6-dependent effect on elongation rate persists during steady-state-induced transcription, reducing the elongation rate from about 1100 to 500 bp/min. Stimulation of Pol II elongation rate by Spt6 is not mediated through transcription factor TFIIS
-
TFB2
-
the essential initiation factor forms a network of interactions with DNA near the transcription start site and facilitates promoter melting but may not be essential for promoter recognition, TFB2 bridges upstream and downstream promoter contacts of the initiation complex, mapping of TFB2-DNA interactions at the transcription start site, overview
-
TFB2M
-
the requirement for TFB2M in transcription of dsDNA is that it can stabilize an incompletely single-stranded template established by negative supercoiling
-
TFIIIE
-
a basal transcription factor, complexes with several ribosomal proteins and enhances tRNA and 5S rRNA transcription of the RNA polymerase, regualtion, overview
-
TFIIS
-
an RNA cleavage stimulatory factor TFIIS. TFIIS can rescue an arrested polymerase by creating a new RNA 3' end at the active site from which transcription can resume, mechanism, overview
-
thermine
-
optimal activity at pH 8.5 is obtained in presence of 18 mM MgCl2, 200 mM KCl, 1 mM thermine and 1 mM spermidine
transcription factor TFIIIB
-
proper initiation by RNA pol III requires the transcription factor TFIIIB. Gene-external U6 snRNA transcription requires TFIIIB consisting of Bdp1, TBP, and Brf2. Transcription from the gene internal tRNA promoter requires TFIIIB composed of Bdp1, TBP, and Brf1. Breast cancer susceptibility gene 1, BRCA1, inhibits TFIIB, which interacts with the BRCA1 C-terminal region domain of Fcp1p, an RNA polymerase II phosphatase, TFIIIB regulation network, overview
-
upstream binding factor
-
CK2
-
is associated with Pol I, the initiation-competent subclass of Pol I, CK2 phosphorylates a number of proteins involved in Pol I transcription and pre-rRNA processing, including UBF, TIF-IA, SL1/TIF-IB, topoisomerase IIa, nucleolin, and nucleophosmin, overview
-
CK2
-
is associated with Pol I, the initiation-competent subclass of Pol I, CK2 phosphorylates a number of proteins involved in Pol I transcription and pre-rRNA processing, including UBF, TIF-IA, SL1/TIF-IB, topoisomerase IIa, nucleolin, and nucleophosmin, overview
-
PAF53
-
a 53-kDa protein that is associated with Pol I, recruitment of Pol I to the pre-initiation complex requires the interaction of UBF with SL1/TIF-IB and with PAF53
-
PAF53
-
a 53-kDa protein that is associated with Pol I, recruitment of Pol I to the pre-initiation complex requires the interaction of UBF with SL1/TIF-IB and with PAF53
-
Rho
-
in response to the Rho termination factor, RNA synthesis ceases and the completed transcript is released
-
Rho
-
in response to the Rho termination factor, RNA synthesis ceases and the completed transcript is released
-
sigma factor
-
a dissociable specificity sigma factor, regulated by factors such as anti-sigma factors, which can sequester sigma factors and prevent core association, and possibly by factors that enhance sigma-core association
-
sigma factor
-
a dissociable specificity sigma factor, regulated by factors such as anti-sigma factors, which can sequester r factors and prevent core association, and possibly by factors that enhance sigma-core association
-
sigma factor
-
required for activity
-
spermidine
-
optimal activity at pH 8.5 is obtained in presence of 18 mM MgCl2, 200 mM KCl, 1 mM thermine and 1 mM spermidine
spermidine
Vectrevirus K1E
-
TAFI protein
-
performs important tasks in transcription complex assembly, mediating specific interactions between the rDNA promoter and Pol I, thereby recruiting Pol I, together with a collection of Pol I-associated factors, to rDNA
-
TAFI protein
-
performs important tasks in transcription complex assembly, mediating specific interactions between the rDNA promoter and Pol I, thereby recruiting Pol I, together with a collection of Pol I-associated factors, to rDNA
-
TIF-IB/SL 1
-
Pol I promoter specificity is conferred by TIF-IB/SL1, a protein complex containing the TATA binding protein and five TATA binding protein-associated factors, including TAFI110/95, TAFI68, TAFI48, TAFI35, and TAFI12
-
TIF-IB/SL 1
-
Pol I promoter specificity is conferred by TIF-IB/SL1, a protein complex containing the TATA binding protein and five TATA binding protein-associated factors, including TAFI110/95, TAFI68, TAFI48, TAFI35, and TAFI12
-
upstream binding factor
-
UBF, activates rRNA gene transcription by several means, for example, by recruiting Pol I to the rDNA promoter, by stabilizing binding of TIF-IB/SL1, and by displacing nonspecific DNA binding proteins such as histone H1. And UBF has additional roles in regulation of Pol I promoter escape and transcription elongation
-
upstream binding factor
-
UBF, activates rRNA gene transcription by several means, for example, by recruiting Pol I to the rDNA promoter, by stabilizing binding of TIF-IB/SL1, and by displacing nonspecific DNA binding proteins such as histone H1. And UBF has additional roles in regulation of Pol I promoter escape and transcription elongation
-
additional information
-
the archaeal Pol II-like transcription apparatus requires the general transcription factors TBP, TFB, TFE and TFS
-
additional information
-
interaction of elongation factors with RNAP, such as NusG and RfaH, affects the frequency and duration of pausing during transcription
-
additional information
-
the enzyme complex requires multiple transcription factors and protein interactions for activity, e.g. Spt6, overview
-
additional information
-
interaction of elongation factors with RNAP, such as NusG and RfaH, affects the frequency and duration of pausing during transcription
-
additional information
-
RNAP contains the vegetative sigma subunit sigma70 (RpoD) and/or the flagellar sigma factor sigma28 (FliA)
-
additional information
-
RNA polymerase complex with associated proteins, overview
-
additional information
-
The activity of basal Pol I factors is regulated by posttranslational modifications
-
additional information
-
the RNA polymerase complex requires several transcription factors for activity, e.g. the general transcription factors, TBP, TFIIA, TFIIB, TFIIF, and TFIIE
-
additional information
-
the archaeal Pol II-like transcription apparatus requires the general transcription factors TBP, TFB, TFE and TFS
-
additional information
-
intermittent hypoxia, a major pathological factor in the development of neural deficits associated with sleep-disordered breathing, regulates RNA polymerase II in hippocampus and prefrontal cortex. Chronic intermittent hypoxia, but not sustained hypoxia, stimulates hydroxylation of Pro1465 in large subunit of RNA polymerase II and phosphorylation of Ser5 of Rpb1, specifically in the CA1 region of the hippocampus and in the prefrontal cortex but not in other regions of the brain, requiring the von Hippel-Lindau tumor suppressor. Mice exposed to chronic IH demonstrated cognitive deficits related to dysfunction in those brain regions
-
additional information
-
The activity of basal Pol I factors is regulated by posttranslational modifications
-
additional information
-
lipopolysaccharides enhance the binding of the enzyme to the iNOS promoter. GlcN enhances RNAPII O-GlcNAcylation, but inhibits iNOS promoter binding
-
additional information
-
mechanism of activation of antibiotic biosynthesis by Nonomuraea rpoB(R), overview
-
additional information
-
the archaeal Pol II-like transcription apparatus requires the general transcription factors TBP, TFB, TFE and TFS
-
additional information
-
the archaeal Pol II-like transcription apparatus requires the general transcription factors TBP, TFB, TFE and TFS
-
additional information
-
the archaeal Pol II-like transcription apparatus requires the general transcription factors TBP, TFB, TFE and TFS
-
additional information
-
Pol III initiates and reinitiates transcription in the absence or presence of transcription factors, during the first transcription cycle transcription factors IIIB and IIIC mainly contribute to the selectivity and not to the rate of Pol III association to the template, while their stable association with the promoter in subsequent cycles strongly contributes to the high rate of transcription reinitiation by Pol III
-
additional information
-
the enzyme complex requires basal transcription factors, i.e. TFIID, TFIIA, TFIIH, and TFIIE, for complete processing of transitions from initiation to elongation, overview
-
additional information
-
the Pol II transcription apparatus requires the transcription factors TBP, TFIIB, TFIIEalpha and TFIIS
-
additional information
-
the Pol II transcription apparatus requires the transcription factors TBP, TFIIB, TFIIEalpha and TFIIS
-
additional information
-
the archaeal Pol II-like transcription apparatus requires the general transcription factors TBP, TFB, TFE and TFS
-
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beta-subunit; gene rpoB, Capsicum annum from Serbia
UniProt
brenda
'Capsicum annuum' phytoplasma Candidatus Phytoplasma solani
beta-subunit; gene rpoB, Capsicum annum from Serbia
UniProt
brenda
beta-subunit; gene rpoB, Catharanthus roseus from Maryland, USA
UniProt
brenda
beta-subunit; gene rpoB, Catharanthus roseus from Maryland, USA
UniProt
brenda
beta-subunit; gene rpoB, Euphorbia pulcherrima from USA
UniProt
brenda
beta-subunit; gene rpoB, Euphorbia pulcherrima from USA
UniProt
brenda
beta-subunit; gene rpoB, Fragaria x ananassa from Lithuania
UniProt
brenda
beta-subunit; gene rpoB, Fragaria x ananassa from Lithuania
UniProt
brenda
'Gomphocarpus physocarpus' phytoplasma
beta-subunit; gene rpoB, Gomphocarpus physocarpus from Australia
UniProt
brenda
'Gomphocarpus physocarpus' phytoplasma Candidatus Phytoplasma australiense
beta-subunit; gene rpoB, Gomphocarpus physocarpus from Australia
UniProt
brenda
beta-subunit; gene rpoB, Heracleum sosnowskyi from Lithuania
UniProt
brenda
beta-subunit; gene rpoB, Heracleum sosnowskyi from Lithuania
UniProt
brenda
beta-subunit; gene rpoB, Lactuca sativa from Ohio, USA
UniProt
brenda
beta-subunit; gene rpoB, Lactuca sativa from Ohio, USA
UniProt
brenda
beta-subunit; gene rpoB, Lycopersicon esculentum from Arkansas, USA
UniProt
brenda
beta-subunit; gene rpoB, Lycopersicon esculentum from Japan
UniProt
brenda
beta-subunit; gene rpoB, Malus domestica from Germany
UniProt
brenda
beta-subunit; gene rpoB, Malus domestica from Germany
UniProt
brenda
beta-subunit; gene rpoB, Oenothera biennis from Lithuania
UniProt
brenda
beta-subunit; gene rpoB, Oenothera biennis from Lithuania
UniProt
brenda
beta-subunit; gene rpoB, Poa pratensis from Lithuania
UniProt
brenda
beta-subunit; gene rpoB, Poa pratensis from Lithuania
UniProt
brenda
beta-subunit; gene rpoB, Prunus persica from Canada
UniProt
brenda
beta-subunit; gene rpoB, Prunus persica from Canada
UniProt
brenda
beta-subunit; gene rpoB, Spiraea sp. from New York, USA
UniProt
brenda
'Spiraea sp.' phytoplasma Spiraea stunt
beta-subunit; gene rpoB, Spiraea sp. from New York, USA
UniProt
brenda
beta-subunit; gene rpoB, Stellaria media from Lithuania
UniProt
brenda
beta-subunit; gene rpoB, Stellaria media from Lithuania
UniProt
brenda
beta-subunit; gene rpoB, Trifolium repens from Canada
UniProt
brenda
beta-subunit; gene rpoB, Trifolium repens from Canada
UniProt
brenda
'Zea mays' phytoplasma
beta-subunit; gene rpoB, Zeamays from Mexico
UniProt
brenda
'Zea mays' phytoplasma Maize bushy stunt
beta-subunit; gene rpoB, Zeamays from Mexico
UniProt
brenda
subunit 6 and subunit beta
UniProt
brenda
-
-
-
brenda
PCC 7120
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
beta-subunit; gene rpoB, Malus domesticus from Germany
UniProt
brenda
beta-subunit; gene rpoB, Malus domesticus from Germany
UniProt
brenda
-
-
-
brenda
-
-
-
brenda
DSM 1731
-
-
brenda
-
-
-
brenda
RNA polymerase I, II and III
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
several strains, gene rpoA
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
Inovirus M13
-
-
-
brenda
genes rpoA, rpoB, rpoC1, and rpoC2 encoding the enzyme subunits
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
the nucleotide sequence of a part, 8334 bp, of the EcoRI fish lymphocystis disease virus DNA fragment B, between the EcoRI site and 259 nucleotides downstream from the second PstI site has been deposited in GenBank accession number: L34213
SwissProt
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
encoded on the linear mitochondrial plasmid
-
-
brenda
P9WGY9: subunit beta, P9WGY7: subunit beta', P9WGZ1: subunit alpha, P9WGY5: omega subunit, P9WGI1: sigma factor SigA, the RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta' and 1 omega subunit. When a sigma factor is associated with the core the holoenzyme is formed, which can initiate transcription
SwissProt
brenda
P9WGY9: subunit beta, P9WGY7: subunit beta', P9WGZ1: subunit alpha, P9WGY5: omega subunit, P9WGI1: sigma factor SigA, the RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta' and 1 omega subunit. When a sigma factor is associated with the core the holoenzyme is formed, which can initiate transcription
SwissProt
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
gene rpoA encoding subunit A
UniProt
brenda
-
-
-
brenda
two RNA polymerase paralogues rpoB(S) and rpoB(R)
-
-
brenda
beta-subunit; gene rpoB, Chrysanthemum coronarium from Japan
UniProt
brenda
beta-subunit; gene rpoB, Chrysanthemum coronarium from Japan
UniProt
brenda
-
-
-
brenda
scorpionfly, collected in June in the village of Toksovo, Leningrad region, Russia
-
-
brenda
beta-subunit; gene rpoB, Arachis hypogaea from China
UniProt
brenda
beta-subunit; gene rpoB, Arachis hypogaea from China
UniProt
brenda
DNA-directed RNA polymerase II subunit RPB6 and subunit RPB10
R4THW7; R4TFI0
UniProt
brenda
gene rpoB encodes the RNA polymerase beta subunit
-
-
brenda
-
-
-
brenda
-
-
-
brenda
PpY101
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-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
Q980R2: subunit A', P58192: subunit A'', Q980R1: subunit B, P95989: subunit D, Q980A3: subunit E', Q9UXD9: subunit F, Q980L5: subunit G, Q980Q9: subunit H, Q97ZJ9: subunit K, Q980K0: subunit L, Q980Z8: subunit N, Q97ZX7: subunit P, Q980B8: subunit 13
UniProt
brenda
-
-
-
brenda
derivative of strain GRF167
-
-
brenda
-
-
-
brenda
-
-
-
brenda
single phage-type RNA polymerase gene rpoT
UniProt
brenda
a deep-sea piezophilic bacterium, genes rpoE2 and rpoE3
-
-
brenda
a deep-sea piezophilic bacterium, genes rpoE2 and rpoE3
-
-
brenda
Spbetavirus SPbeta
-
SwissProt
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
gene TON-0309
UniProt
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
HB8
-
-
brenda
-
-
-
brenda
P21603: DNA-directed RNA polymerase 30 kDa polypeptide
SwissProt
brenda
-
-
-
brenda
Vectrevirus K1E
gene k1ep
UniProt
brenda
gene rpoB encodes the RNA polymerase beta subunit
UniProt
brenda
gene rpoB encodes the RNA polymerase beta subunit
UniProt
brenda
gene rpoB encodes the RNA polymerase beta subunit
-
-
brenda
gene rpoB encodes the RNA polymerase beta subunit
-
-
brenda
gene rpoB encodes the RNA polymerase beta subunit
-
-
brenda
gene rpoB encodes the RNA polymerase beta subunit
-
-
brenda
gene rpoB encodes the RNA polymerase beta subunit
-
-
brenda
gene rpoB encodes the RNA polymerase beta subunit
-
-
brenda
gene rpoB encodes the RNA polymerase beta subunit
-
-
brenda
-
-
-
brenda
-
-
-
brenda
Zindervirus SP6
-
-
-
brenda
beta-subunit; gene rpoB, Asclepias syriaca from New York, USA
UniProt
brenda
beta-subunit; gene rpoB, Asclepias syriaca from Virginia, USA
UniProt
brenda
beta-subunit; gene rpoB, Asclepias syriaca from New York, USA
UniProt
brenda
beta-subunit; gene rpoB, Asclepias syriaca from Virginia, USA
UniProt
brenda
beta-subunit; gene rpoB, Lycopersicon esculentum from Arkansas, USA
UniProt
brenda
beta-subunit; gene rpoB, Lycopersicon esculentum from Japan
UniProt
brenda
-
643564, 643570, 643584, 643587, 660691, 661201, 662629, 663386, 673217, 676146, 702224, 702625, 703353, 703357, 705530, 706807, 706873, 721305, 723296, 761982, 761990, 762047 -
-
brenda
alpha-subunit
SwissProt
brenda
DNA-directed RNA polymerase subunits beta, beta', and alpha encoded by genes rpoC, rpoB, and rpoA; genes rpoC, rpoB, and rpoA
UniProt
brenda
P0A8T7: rpoC, DNA-directed RNA polymerase subunit beta, P0A8V2: rpoB, DNA-directed RNA polymerase subunit beta, P0A7Z4: rpoA, DNA-directed RNA polymerase subunit alpha, P0A800: rpoZ, DNA-directed RNA polymerase subunit omega
SwissProt
brenda
strains JCB387 and M182
-
-
brenda
alpha-subunit
SwissProt
brenda
P0A8T7: rpoC, DNA-directed RNA polymerase subunit beta, P0A8V2: rpoB, DNA-directed RNA polymerase subunit beta, P0A7Z4: rpoA, DNA-directed RNA polymerase subunit alpha, P0A800: rpoZ, DNA-directed RNA polymerase subunit omega
SwissProt
brenda
-
-
-
brenda
-
Uniprot
brenda
-
-
-
brenda
-
Uniprot
brenda
-
-
-
brenda
-
643551, 643555, 677248, 692483, 694828, 701717, 703150, 703354, 703458, 703854, 704096, 704671, 705139, 705704, 705982, 721721, 722993, 723183, 723636, 738010, 738671 -
-
brenda
-
SwissProt
brenda
-
-
-
brenda
male C57Bl6 mice
-
-
brenda
-
-
-
brenda
A0QSL8: rpoA, subunit alpha, P60281: rpoB, subunit beta, A0QS66: rpoC, subunit beta', A0QWT1: rpoZ, subunit omega
SwissProt
brenda
P60281: beta subunit, A0QS66: beta' subunit, A0QSL8: alpha subunit, A0QWT1: omega subunit, A0QW02: sigma factor The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta' and 1 omega subunit. When a sigma factor is associated with the core the holoenzyme is formed, which can initiate transcription
SwissProt
brenda
A0QSL8: rpoA, subunit alpha, P60281: rpoB, subunit beta, A0QS66: rpoC, subunit beta', A0QWT1: rpoZ, subunit omega
SwissProt
brenda
P60281: beta subunit, A0QS66: beta' subunit, A0QSL8: alpha subunit, A0QWT1: omega subunit, A0QW02: sigma factor The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta' and 1 omega subunit. When a sigma factor is associated with the core the holoenzyme is formed, which can initiate transcription
SwissProt
brenda
-
SwissProt
brenda
-
-
-
brenda
-
-
-
brenda
strain PAO1, ATCC 15692, and strain W1485
-
-
brenda
-
-
-
brenda
PpY101
-
-
brenda
-
-
-
brenda
-
UniProt
brenda
13-subunit enzyme
UniProt
brenda
-
UniProt
brenda
13-subunit enzyme
UniProt
brenda
-
-
-
brenda
Q980R2: subunit A', P58192: subunit A'', Q980R1: subunit B, P95989: subunit D, Q980A3: subunit E', Q9UXD9: subunit F, Q980L5: subunit G, Q980Q9: subunit H, Q97ZJ9: subunit K, Q980K0: subunit L, Q980Z8: subunit N, Q97ZX7: subunit P, Q980B8: subunit 13
UniProt
brenda
-
643554, 643555, 643577, 643578, 643580, 643581, 662831, 663216, 691700, 694328, 701466, 702030, 702171, 702625, 703147, 703353, 703354, 703448 -
-
brenda
-
UniProt
brenda
-
-
-
brenda
derivative of strain GRF167
-
-
brenda
gene RPO41
-
-
brenda
strains YZS84 and YDP19
-
-
brenda
-
-
-
brenda
-
UniProt
brenda
-
-
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brenda
strain DSM 639
-
-
brenda
subunit E
SwissProt
brenda
subunit H
SwissProt
brenda
subunit L; strain DSM 639
SwissProt
brenda
subunit M; strain DSM 639
SwissProt
brenda
-
-
-
brenda
subunit H
SwissProt
brenda
-
-
-
brenda
HB8
-
-
brenda
Q5SHR6: subunit alpha, Q8RQE9: subunit beta, Q8RQE8: subunit beta', Q8RQE7: subunit omega
SwissProt
brenda
-
-
-
brenda
procyclic, tsetse midgut wild-type form, Lister 427
-
-
brenda
-
-
-
brenda
P21603: DNA-directed RNA polymerase 30 kDa polypeptide
SwissProt
brenda
rpoA, alpha-subunit; pv. campestris
UniProt
brenda
rpoB; pv. campestris
UniProt
brenda
rpoC; pv. campestris
UniProt
brenda
rpoD; pv. campestris
UniProt
brenda
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drug target
sorangicin A inhibits the wild-type and mutant RNA polymerase through different mechanisms. It has a better pharmacokinetic profile than rifampicin, making it a suitable starting molecule to design drugs to be used for the treatment of tuberculosis patients with comorbidities who require multiple medications
drug target
sorangicin A inhibits the wild-type and mutant RNA polymerase through different mechanisms. It has a better pharmacokinetic profile than rifampicin, making it a suitable starting molecule to design drugs to be used for the treatment of tuberculosis patients with comorbidities who require multiple medications
drug target
-
the template-DNA binding site is a target site for developing antibacterial agents
drug target
the template-DNA binding site is a target site for developing antibacterial agents
drug target
-
sorangicin A inhibits the wild-type and mutant RNA polymerase through different mechanisms. It has a better pharmacokinetic profile than rifampicin, making it a suitable starting molecule to design drugs to be used for the treatment of tuberculosis patients with comorbidities who require multiple medications
-
drug target
-
sorangicin A inhibits the wild-type and mutant RNA polymerase through different mechanisms. It has a better pharmacokinetic profile than rifampicin, making it a suitable starting molecule to design drugs to be used for the treatment of tuberculosis patients with comorbidities who require multiple medications
-
evolution
-
human mitochondrial RNA polymerase is distantly related to the bacteriophage T7 class of single-subunit RNAPs with a probably similar mechanisms for nucleotide binding, substrate selection and catalysis/nucleotidyl transfer. The C-terminal domain contains the regions of highest similarity to the phage RNAPs. Early in the evolution of eukaryotes there has been a switch from a multi-subunit prokaryotic polymerase to a single-subunit, phage-derived polymerase, encoded in the nuclear genome and imported into the mitochondria, to serve as the transcriptase of the mitochondrial genome. The POLRMT CTD is characteristic of the Pol I family of nucleic acid polymerases, typically described as resembling the shape of a cupped right hand, containing the fingers, palm and thumb subdomains. The palm subdomain contains several key structural motifs that are highly conserved among the different classes of nucleic acid polymerases
evolution
-
Rpo41 utilizes a promoter recognition loop to bind and recognize its promoter, analogous to the use of the specificity loop by T7 RNAP for this purpose
evolution
genotyping and phylogenetic analysis of gene rpoB encoding the beta subunit of the DNA-directed RNA polymerase of phytoplasmas from different plant origins, detailed overview
evolution
genotyping and phylogenetic analysis of gene rpoB encoding the beta subunit of the DNA-directed RNA polymerase of phytoplasmas from different plant origins, detailed overview
evolution
genotyping and phylogenetic analysis of gene rpoB encoding the beta subunit of the DNA-directed RNA polymerase of phytoplasmas from different plant origins, detailed overview
evolution
genotyping and phylogenetic analysis of gene rpoB encoding the beta subunit of the DNA-directed RNA polymerase of phytoplasmas from different plant origins, detailed overview
evolution
genotyping and phylogenetic analysis of gene rpoB encoding the beta subunit of the DNA-directed RNA polymerase of phytoplasmas from different plant origins, detailed overview
evolution
genotyping and phylogenetic analysis of gene rpoB encoding the beta subunit of the DNA-directed RNA polymerase of phytoplasmas from different plant origins, detailed overview
evolution
genotyping and phylogenetic analysis of gene rpoB encoding the beta subunit of the DNA-directed RNA polymerase of phytoplasmas from different plant origins, detailed overview
evolution
genotyping and phylogenetic analysis of gene rpoB encoding the beta subunit of the DNA-directed RNA polymerase of phytoplasmas from different plant origins, detailed overview
evolution
genotyping and phylogenetic analysis of gene rpoB encoding the beta subunit of the DNA-directed RNA polymerase of phytoplasmas from different plant origins, detailed overview
evolution
genotyping and phylogenetic analysis of gene rpoB encoding the beta subunit of the DNA-directed RNA polymerase of phytoplasmas from different plant origins, detailed overview
evolution
genotyping and phylogenetic analysis of gene rpoB encoding the beta subunit of the DNA-directed RNA polymerase of phytoplasmas from different plant origins, detailed overview
evolution
'Gomphocarpus physocarpus' phytoplasma
genotyping and phylogenetic analysis of gene rpoB encoding the beta subunit of the DNA-directed RNA polymerase of phytoplasmas from different plant origins, detailed overview
evolution
genotyping and phylogenetic analysis of gene rpoB encoding the beta subunit of the DNA-directed RNA polymerase of phytoplasmas from different plant origins, detailed overview
evolution
genotyping and phylogenetic analysis of gene rpoB encoding the beta subunit of the DNA-directed RNA polymerase of phytoplasmas from different plant origins, detailed overview
evolution
genotyping and phylogenetic analysis of gene rpoB encoding the beta subunit of the DNA-directed RNA polymerase of phytoplasmas from different plant origins, detailed overview
evolution
genotyping and phylogenetic analysis of gene rpoB encoding the beta subunit of the DNA-directed RNA polymerase of phytoplasmas from different plant origins, detailed overview
evolution
'Zea mays' phytoplasma
genotyping and phylogenetic analysis of gene rpoB encoding the beta subunit of the DNA-directed RNA polymerase of phytoplasmas from different plant origins, detailed overview
evolution
genotyping and phylogenetic analysis of gene rpoB encoding the beta subunit of the DNA-directed RNA polymerase of phytoplasmas from different plant origins, detailed overview
evolution
genotyping and phylogenetic analysis of gene rpoB encoding the beta subunit of the DNA-directed RNA polymerase of phytoplasmas from different plant origins, detailed overview
evolution
genotyping and phylogenetic analysis of gene rpoB encoding the beta subunit of the DNA-directed RNA polymerase of phytoplasmas from different plant origins, detailed overview
evolution
-
the rpo genes that encode the enzyme subunits, rpoA, rpoB, rpoC1, and rpoC2, are relatively rapidly evolving sequences. Determination of the rate of the molecular evolution of rpo genes and to evaluation as phylogenetic markers on the example of the genus Lamium, Lamiaceae, represented by 66 specimens. Distribution of substitution rates across rpo genes as calculated in HyPhy using the GTR model of evolution, overview. The process of evolution of the RNA polymerase type I enzyme in genus Lamium is due not only to the genetic drift
evolution
Spbetavirus SPbeta
YonO and related proteins present in various bacteria and bacteriophages have diverged from msRNAPs before the Last Universal Common Ancestor, and, thus, may resemble the single-subunit ancestor of all multi-subunit RNA polymerases
evolution
-
genotyping and phylogenetic analysis of gene rpoB encoding the beta subunit of the DNA-directed RNA polymerase of phytoplasmas from different plant origins, detailed overview
-
evolution
-
genotyping and phylogenetic analysis of gene rpoB encoding the beta subunit of the DNA-directed RNA polymerase of phytoplasmas from different plant origins, detailed overview
-
evolution
-
genotyping and phylogenetic analysis of gene rpoB encoding the beta subunit of the DNA-directed RNA polymerase of phytoplasmas from different plant origins, detailed overview
-
evolution
-
genotyping and phylogenetic analysis of gene rpoB encoding the beta subunit of the DNA-directed RNA polymerase of phytoplasmas from different plant origins, detailed overview
-
evolution
-
genotyping and phylogenetic analysis of gene rpoB encoding the beta subunit of the DNA-directed RNA polymerase of phytoplasmas from different plant origins, detailed overview
-
evolution
-
genotyping and phylogenetic analysis of gene rpoB encoding the beta subunit of the DNA-directed RNA polymerase of phytoplasmas from different plant origins, detailed overview
-
evolution
-
genotyping and phylogenetic analysis of gene rpoB encoding the beta subunit of the DNA-directed RNA polymerase of phytoplasmas from different plant origins, detailed overview
-
evolution
-
genotyping and phylogenetic analysis of gene rpoB encoding the beta subunit of the DNA-directed RNA polymerase of phytoplasmas from different plant origins, detailed overview
-
evolution
-
genotyping and phylogenetic analysis of gene rpoB encoding the beta subunit of the DNA-directed RNA polymerase of phytoplasmas from different plant origins, detailed overview
-
evolution
-
genotyping and phylogenetic analysis of gene rpoB encoding the beta subunit of the DNA-directed RNA polymerase of phytoplasmas from different plant origins, detailed overview
-
evolution
'Spiraea sp.' phytoplasma Spiraea stunt
-
genotyping and phylogenetic analysis of gene rpoB encoding the beta subunit of the DNA-directed RNA polymerase of phytoplasmas from different plant origins, detailed overview
-
evolution
-
genotyping and phylogenetic analysis of gene rpoB encoding the beta subunit of the DNA-directed RNA polymerase of phytoplasmas from different plant origins, detailed overview
-
evolution
-
genotyping and phylogenetic analysis of gene rpoB encoding the beta subunit of the DNA-directed RNA polymerase of phytoplasmas from different plant origins, detailed overview
-
evolution
-
genotyping and phylogenetic analysis of gene rpoB encoding the beta subunit of the DNA-directed RNA polymerase of phytoplasmas from different plant origins, detailed overview
-
evolution
'Zea mays' phytoplasma Maize bushy stunt
-
genotyping and phylogenetic analysis of gene rpoB encoding the beta subunit of the DNA-directed RNA polymerase of phytoplasmas from different plant origins, detailed overview
-
evolution
'Gomphocarpus physocarpus' phytoplasma Candidatus Phytoplasma australiense
-
genotyping and phylogenetic analysis of gene rpoB encoding the beta subunit of the DNA-directed RNA polymerase of phytoplasmas from different plant origins, detailed overview
-
evolution
-
genotyping and phylogenetic analysis of gene rpoB encoding the beta subunit of the DNA-directed RNA polymerase of phytoplasmas from different plant origins, detailed overview
-
evolution
-
genotyping and phylogenetic analysis of gene rpoB encoding the beta subunit of the DNA-directed RNA polymerase of phytoplasmas from different plant origins, detailed overview
-
evolution
'Capsicum annuum' phytoplasma Candidatus Phytoplasma solani
-
genotyping and phylogenetic analysis of gene rpoB encoding the beta subunit of the DNA-directed RNA polymerase of phytoplasmas from different plant origins, detailed overview
-
evolution
-
genotyping and phylogenetic analysis of gene rpoB encoding the beta subunit of the DNA-directed RNA polymerase of phytoplasmas from different plant origins, detailed overview
-
evolution
-
genotyping and phylogenetic analysis of gene rpoB encoding the beta subunit of the DNA-directed RNA polymerase of phytoplasmas from different plant origins, detailed overview
-
malfunction
-
DNA topoisomerase I inhibition by camptothecin induces escape of RNA polymerase II from promoter-proximal pause site, antisense transcription and histone acetylation at the human HIF-1alpha gene locus
malfunction
-
reverse translocation, i.e. backtracking, by a distance of one or more nucleotides disrupts the configuration of the catalytic center, leading to a temporary, spontaneously resolved, halt of the RNAP, called pausing, or to a transition into an irreversible arrested state. The latter can be restored to functionality by the endonucleolytic cleavage of the RNA or by pushing the backtracked complex from behind. Non-backtracked paused complexes are also described for bacterial RNAPs, where addition of the incoming NTP is hindered owing to isomerization of the active site into an inactive conformation
malfunction
-
reverse translocation, i.e. backtracking, by a distance of one or more nucleotides disrupts the configuration of the catalytic center, leading to a temporary, spontaneously resolved, halt of the RNAP, called pausing, or to a transition into an irreversible arrested state. The latter can be restored to functionality by the endonucleolytic cleavage of the RNA or by pushing the backtracked complex from behind. Non-backtracked paused complexes are also described for bacterial RNAPs, where addition of the incoming NTP is hindered owing to isomerization of the active site into an inactive conformation
malfunction
-
reverse translocation, i.e. backtracking, by a distance of one or more nucleotides disrupts the configuration of the catalytic center, leading to a temporary, spontaneously resolved, halt of the RNAP, called pausing, or to a transition into an irreversible arrested state. The latter can be restored to functionality by the endonucleolytic cleavage of the RNA or by pushing the backtracked complex from behind. Non-backtracked paused complexes are also described for bacterial RNAPs, where addition of the incoming NTP is hindered owing to isomerization of the active site into an inactive conformation
malfunction
-
reverse translocation, i.e. backtracking, by a distance of one or more nucleotides disrupts the configuration of the catalytic center, leading to a temporary, spontaneously resolved, halt of the RNAP, called pausing, or to a transition into an irreversible arrested state. The latter can be restored to functionality by the endonucleolytic cleavage of the RNA or by pushing the backtracked complex from behind. Non-backtracked paused complexes are also described for bacterial RNAPs, where addition of the incoming NTP is hindered owing to isomerization of the active site into an inactive conformation
malfunction
-
reverse translocation, i.e. backtracking, by a distance of one or more nucleotides disrupts the configuration of the catalytic center, leading to a temporary, spontaneously resolved, halt of the RNAP, called pausing, or to a transition into an irreversible arrested state. The latter can be restored to functionality by the endonucleolytic cleavage of the RNA or by pushing the backtracked complex from behind. Non-backtracked paused complexes are also described for bacterial RNAPs, where addition of the incoming NTP is hindered owing to isomerization of the active site into an inactive conformation
malfunction
-
at lower concentrations, pyrimidine nucleoside analogs have the potential to more easily inhibit mitochondrial transcription and mediate toxicity, given the ability to be readily phosphorylated and serve as efficient substrates for the enzyme
malfunction
-
mutant Sc Rpb2 R512C is slow in elongation
malfunction
-
R428A RNAP is instable
malfunction
-
replication intermediates associated with an unusually prolonged delay in the initiation of second strand DNA synthesis are enhanced by combined shRNA and dsRNA POLRMT gene silencing
malfunction
-
suppression of subunit RPC32alpha expression by siRNAs impedes anchorage-independent growth of HeLa cells, whereas ectopic expression of RPC32alpha in IMR90 fibroblasts enhances cell transformation and dramatically changes the expression of several tumor-related mRNAs and that of a subset of Pol III RNAs
malfunction
-
rDNA silencing is attenuated by loss of Pol I subunits or insertion of an ectopic Pol I terminator within the adjacent rDNA gene. Silencing left of the rDNA array is naturally attenuated by the presence of only one intact Fob1 binding site (Ter2). Repair of the 2nd Fob1 binding site (Ter1) dramatically strengthens silencing such that it is no longer impacted by local Pol I transcription defects. Global loss of Pol I activity, negatively affects Fob1 association with the rDNA. Loss of Ter2 almost completely eliminates localized silencing, but is restored by artificially targeting Fob1 or Sir2 as Gal4 DNA binding domain fusions
malfunction
-
rDNA silencing is attenuated by loss of Pol I subunits or insertion of an ectopic Pol I terminator within the adjacent rDNA gene. Silencing left of the rDNA array is naturally attenuated by the presence of only one intact Fob1 binding site (Ter2). Repair of the 2nd Fob1 binding site (Ter1) dramatically strengthens silencing such that it is no longer impacted by local Pol I transcription defects. Global loss of Pol I activity, negatively affects Fob1 association with the rDNA. Loss of Ter2 almost completely eliminates localized silencing, but is restored by artificially targeting Fob1 or Sir2 as Gal4 DNA binding domain fusions
-
physiological function
-
detailed overview
physiological function
-
detailed overview
physiological function
-
Pol II is the eukaryotic enzyme that is responsible for transcribing all protein-coding genes into mRNA. The mRNA-transcription cycle can be divided into three stages: initiation, elongation and termination. During elongation, Pol II moves along a DNA template and synthesizes a complementary RNA chain in a processive manner
physiological function
-
POLRMT is a key molecule of the core complex of the mitochondrial transcription machinery which assembles at promoter sequences on both strands of mtDNA, termed the L-strand promoter and H-strand promoter
physiological function
-
RNA pol III is involved in regulating the growth rate of cells
physiological function
-
RNA polymerase II has a regulatory function on nucleoside triphosphate synthesis, mutations of RNA polymerase II activate key genes of the nucleoside triphosphate biosynthetic pathways, overview
physiological function
RNA polymerase II is the central enzyme of eukaryotic gene expression machinery, analysis of regulation mechanisms of transcription via protein-protein interactions within the Pol II apparatus, overview
physiological function
-
RNAP is an exceptionally complex enzyme that can be thought of as the engine of gene expression
physiological function
-
RNAP is an exceptionally complex enzyme that can be thought of as the engine of gene expression
physiological function
-
RNAP-II is essential for gene expression in metazoa
physiological function
-
the enzyme can be involved in both replication and integration processes of these plasmid in the mitochondrial genome
physiological function
-
the enzyme from Zea mays exhibits a role in genome-wide and small RNA-associated gene silencing, but is not essential for the plant, PolIV is involved in paramutation, an inherited epigenetic change facilitated by an interaction of two alleles, overview
physiological function
-
increased Pol III transcription accompanies or causes cell transformation. RPC32beta subunit-containing isozyme Pol IIIbeta is ubiquitously expressed and essential for growth of human cells. RPC32alpha subunit-containing isozyme Pol IIIalpha is dispensable for cell survival, with expression being restricted to undifferentiated ES cells and to tumor cells. Dramatic changes in 5S RNA, U6 RNA, and 7SKRNA expression are specifically caused by ectopic expression of RPC32alpha and not due to a general deregulation of transcription
physiological function
-
mitochondrial DNA is replicated by a unique enzymatic machinery involving the POLRMT-mediated initiation of primer synthesis from a poly-dT stretch in the single-stranded loop region of the light-strand origin of DNA replication, when the single-stranded origin of DNA replication is exposed and adopts a stem-loop structure. The poly-dT repeat region of origin of DNA replication is an essential element for primer synthesis. POLRMT can function as an origin-specific primase in mammalian mitochondria, overview
physiological function
-
the enzyme activates genes for high affinity nutrient scavenging and motility
physiological function
-
the enzyme is required for expression of 13 subunits of the respiratory chain complexes involved in oxidative phosphorylation and rRNAs and tRNAs, required for mitochondrial translation. Rpo41 can initiate transcription from negatively supercoiled templates and pre-melted promoter substrates in the absence of the yeast mitochondrial transcription factor, Mtf1. Mechanisms and species specificity for promoter recognition, overview
physiological function
-
the enzyme is required for expression of 13 subunits of the respiratory chain complexes involved in oxidative phosphorylation and two rRNAs and 22 tRNAs, required for mitochondrial translation. In addition to its role in transcription, in the mitochondria, POLRMT serves as the primase for mitochondrial DNA replication. Mechanisms and species specificity for promoter recognition, overview. Complex formation between the enzyme and the other transcription factors at the promoter, the structural elements of the enzyme are repositioned in such a way as to allow for specific promoter recognition, open complex formation and transcription initiation
physiological function
-
RNA polymerase binds to the promoter regions of the gdh, rrnC, and rrnE genes encoding glutamate dehydrogenase and rRNA and activates their transcription
physiological function
-
active Pol I transcription is critical for silencing of Pol II transcription within the rDNA. Sir2 is recruited to the rDNA promoter through interactions with RNA polymerase I, Sir2 suppresses RNA polymerase II (Pol II)-transcribed genes embedded within the yeast rDNA locus, i.e. rDNA silencing. Fob1 and Pol Imake independent contributions to establishment of silencing, though Pol I also reinforces Fob1-dependent silencing
physiological function
-
basal transcriptional activity and RNAPII DNA binding might be associated with the O-GlcNAcylation and/or phosphorylation state of RNAPII, which can involve changed association with other transcription factors during inflammation
physiological function
-
binding of the termination factor Nsi1 to its cognate DNA site is sufficient to terminate RNA polymerase I transcription in vitro and to induce termination in vivo. Nsi1 contains Myb-like DNA binding domains and associates in vivo near the 3' end of rRNA genes to rDNA
physiological function
plastid genes are transcribed by two types of RNA polymerases: a plastid-encoded eubacterial-type RNA polymerase and nuclear-encoded phage-type RNA polymerases, spatio-temporal expression of plastid RNA polymerase. The association of plastid RNA polymerase with photosynthesis-related genes is reduced during the dark period, indicating that plastome-wide plastid RNA polymerase-DNA association is a light-dependent process
physiological function
-
RNA polymerase III regulates the presence of cytosolic RNA:DNA hybrids and miRNA biogenesis in various human cells. RNA:DNA hybrids exist in the cytosol of various human cells and are mediated by RNA polymerase III, which regulates the microRNA machinery, cytosolic RNA:DNA hybrids may have physiological relevance to miRNA machinery and RNA transport, miRNA expression analysis, RNA transport and mRNA surveillance pathways are potential targets of Pol III-modulated miRNAs, overview. Inhibition of the DNA damage response has no effect on the presence of RNA:DNA hybrids in the cytosol, and the levels of cytosolic RNA:DNA hybrids are not modulated by genotoxic replication inhibitors
physiological function
RNA polymerase plays a crucial role in gene expression in all organisms. It is a multiprotein complex that produces primary transcript RNA from a DNA template
physiological function
-
RNA polymerase type I (plastid-encoded polymerase, PEP) is one of the key chloroplast enzymes
physiological function
the enzyme subunits interact with CedA, a multi-copy suppressor which represses the dnaAcos inhibition of cell division. DnaAcos is a mutant of the initiator DnaA that causes overinitiation of chromosome replication in Escherichia coli resulting in inhibition of cell division. Determination of the binding site of CedA for RNA polymerase and examination of the binding functions involved in cell division reactivation
physiological function
-
the yeast mitochondrial RNA polymerase and transcription factor complex catalyzes efficient priming of DNA synthesis on single-stranded DNA. Primases are specialized DNA-dependent RNA polymerases that synthesize short oligoribonucleotides de novo on single-stranded (ss) DNA templates
physiological function
gene transcription is carried out by multi-subunit RNA polymerase. Transcription initiation is a dynamic multi-step process that involves the opening of the double-stranded DNA to form a transcription bubble and delivery of the template strand deep into the RNAP for RNA synthesis. Transcription bubble is stabilized by a helix separating the two DNA strands
physiological function
Spbetavirus SPbeta
the enzyme specifically transcribes its late genes of Bacillus phage SPbeta
physiological function
-
transcriptional bursting is caused by interplay between RNA polymerases on DNA
physiological function
-
binding of the termination factor Nsi1 to its cognate DNA site is sufficient to terminate RNA polymerase I transcription in vitro and to induce termination in vivo. Nsi1 contains Myb-like DNA binding domains and associates in vivo near the 3' end of rRNA genes to rDNA
-
physiological function
-
gene transcription is carried out by multi-subunit RNA polymerase. Transcription initiation is a dynamic multi-step process that involves the opening of the double-stranded DNA to form a transcription bubble and delivery of the template strand deep into the RNAP for RNA synthesis. Transcription bubble is stabilized by a helix separating the two DNA strands
-
physiological function
-
active Pol I transcription is critical for silencing of Pol II transcription within the rDNA. Sir2 is recruited to the rDNA promoter through interactions with RNA polymerase I, Sir2 suppresses RNA polymerase II (Pol II)-transcribed genes embedded within the yeast rDNA locus, i.e. rDNA silencing. Fob1 and Pol Imake independent contributions to establishment of silencing, though Pol I also reinforces Fob1-dependent silencing
-
additional information
-
structure-based analysis of the evolution of archaeal and eukaryotic DNA-dependent RNA polymerases, overview
additional information
-
structure-based analysis of the evolution of archaeal and eukaryotic DNA-dependent RNA polymerases, overview
additional information
-
structure-based analysis of the evolution of archaeal and eukaryotic DNA-dependent RNA polymerases, overview
additional information
-
structure-based analysis of the evolution of archaeal and eukaryotic DNA-dependent RNA polymerases, overview
additional information
-
structure-based analysis of the evolution of archaeal and eukaryotic DNA-dependent RNA polymerases, overview
additional information
-
structure-based analysis of the evolution of archaeal and eukaryotic DNA-dependent RNA polymerases, overview
additional information
-
structure-based analysis of the evolution of archaeal and eukaryotic DNA-dependent RNA polymerases, overview
additional information
-
structure-based analysis of the evolution of archaeal and eukaryotic DNA-dependent RNA polymerases, overview
additional information
-
structure-based analysis of the evolution of archaeal and eukaryotic DNA-dependent RNA polymerases, overview
additional information
-
structure-based analysis of the evolution of archaeal and eukaryotic DNA-dependent RNA polymerases, overview
additional information
-
in vitro assembly of Sc RNAP II ternary elongation complexes, overview. RNA polymerase in a catalytic conformation demonstrates that the active site dNMP-NTP base pair must be substantially dehydrated to support full active site closing and optimum conditions for phosphodiester bond synthesis. An active site latch assembly that includes a key trigger helix residue beta' H1242 and highly conserved active site residues beta E445 and R557 appears to help regulate active site hydration/dehydration. Molecular dynamics simulations, overview
additional information
-
modeling of Tt RNAP TEC containing a closed, catalytic trigger helix conformation. RNA polymerase in a catalytic conformation demonstrates that the active site dNMP-NTP base pair must be substantially dehydrated to support full active site closing and optimum conditions for phosphodiester bond synthesis. An active site latch assembly that includes a key trigger helix residue beta' H1242 and highly conserved active site residues beta E445 and R557 appears to help regulate active site hydration/dehydration. Molecular dynamics simulations, overview
additional information
-
POLRMT distinct mechanisms for promoter recognition and transcription initiation, kinetic mechanism for POLRMT-catalyzed nucleotide incorporation, and structure-function relationship, nucleotidyl transfer and the nucleotide-addition cycle, detailed overview
additional information
DNA-dependent RNA polymerase (RNAP) genes are universal in microbes and conserved in giant viruses and may replace rDNA for identifying microbes
additional information
R4THW7; R4TFI0
DNA-dependent RNA polymerase (RNAP) genes are universal in microbes and conserved in giant viruses and may replace rDNA for identifying microbes
additional information
-
DNA-dependent RNA polymerase (RNAP) genes are universal in microbes and conserved in giant viruses and may replace rDNA for identifying microbes
additional information
-
a single-molecule fluorescence assay is established to study bacterial transcription termination dynamics
additional information
-
RNA polymerase is a major target of gene regulation
additional information
RNA polymerase is a major target of gene regulation
additional information
-
studies on the transcription mechanism show transcription reinitiation by recycling RNA polymerase that diffuses on DNA after releasing terminated RNA
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101000
-
1 * 122000 + 1 * 101000 + 1 * 44000 + 1 * 32000 + 1 * 24000 + 1 * 17500 + 1 * 13800 + 4 * 11800 + 1 * 11200 + 1 * 10800, SDS-PAGE
105000
-
x * 146000, beta and beta comigrate, + x * 105000, main sigma factor, + x * 40000, alpha, SDS-PAGE
10800
-
1 * 122000 + 1 * 101000 + 1 * 44000 + 1 * 32000 + 1 * 24000 + 1 * 17500 + 1 * 13800 + 4 * 11800 + 1 * 11200 + 1 * 10800, SDS-PAGE
110000
-
x * 120000 + x * 110000 + x * 95000 + x * 84000 + x * 81000 + x * 75000 + x * 54000 + x * 51000 + x * 42000 + x * 35000, the 110000 Da polypeptide binds nucleoside triphosphates, the 42000 Da polypeptide cross-reacts with antiserum raised to the plastid endoded rpoA gene product, SDS-PAGE
11200
-
1 * 122000 + 1 * 101000 + 1 * 44000 + 1 * 32000 + 1 * 24000 + 1 * 17500 + 1 * 13800 + 4 * 11800 + 1 * 11200 + 1 * 10800, SDS-PAGE
11800
-
1 * 122000 + 1 * 101000 + 1 * 44000 + 1 * 32000 + 1 * 24000 + 1 * 17500 + 1 * 13800 + 4 * 11800 + 1 * 11200 + 1 * 10800, SDS-PAGE
120000
-
x * 120000 + x * 110000 + x * 95000 + x * 84000 + x * 81000 + x * 75000 + x * 54000 + x * 51000 + x * 42000 + x * 35000, the 110000 Da polypeptide binds nucleoside triphosphates, the 42000 Da polypeptide cross-reacts with antiserum raised to the plastid endoded rpoA gene product, SDS-PAGE
122000
-
1 * 122000 + 1 * 101000 + 1 * 44000 + 1 * 32000 + 1 * 24000 + 1 * 17500 + 1 * 13800 + 4 * 11800 + 1 * 11200 + 1 * 10800, SDS-PAGE
125000
-
x * 185000 + x * 125000 + x * 47000 + x * 30000 + x * 93000, SDS-PAGE
13000
-
x * 210000 + x * 150000 + x * 40000 + x * 34000 + x * 33000 + x * 25000 + x * 20000 + x * 16000 + x * 15000 + x * 13500 + x * 13000, the enzyme contains more than eleven polypeptides, SDS-PAGE
130000
-
x * 130000, beta-subunit, plus x * 140000, beta-subunit, SDS-PAGE
134000
-
x * 161000 + x * 134000 + x * 72000 + x * 41000 + x * 91000, SDS-PAGE
13500
-
x * 210000 + x * 150000 + x * 40000 + x * 34000 + x * 33000 + x * 25000 + x * 20000 + x * 16000 + x * 15000 + x * 13500 + x * 13000, the enzyme contains more than eleven polypeptides, SDS-PAGE
13800
-
1 * 122000 + 1 * 101000 + 1 * 44000 + 1 * 32000 + 1 * 24000 + 1 * 17500 + 1 * 13800 + 4 * 11800 + 1 * 11200 + 1 * 10800, SDS-PAGE
141000
-
beta,beta,sigma,alpha occur with a stoichiometric ratio of 1:1:1:2, x * 184000 + x * 141000 + x * 55000 + x * 45000, SDS-PAGE
142000
-
betax,betax,sigmax,alphax, x * 148000 + x * 142000 + x * 85000 + x * 34500, SDS-PAGE
146000
-
x * 146000, beta and beta comigrate, + x * 105000, main sigma factor, + x * 40000, alpha, SDS-PAGE
147000
-
x * 151000 + x * 147000 + x * 55000 + x * 42000, SDS-PAGE
15000
-
x * 210000 + x * 150000 + x * 40000 + x * 34000 + x * 33000 + x * 25000 + x * 20000 + x * 16000 + x * 15000 + x * 13500 + x * 13000, the enzyme contains more than eleven polypeptides, SDS-PAGE
150000
-
x * 210000 + x * 150000 + x * 40000 + x * 34000 + x * 33000 + x * 25000 + x * 20000 + x * 16000 + x * 15000 + x * 13500 + x * 13000, the enzyme contains more than eleven polypeptides, SDS-PAGE
156000
-
betax,betax,alphax,sigmax, x * 156000 + x * 151000 + x * 87000 + x * 42000, SDS-PAGE
157000
-
beta,beta,sigma,alpha. Subunit stoichiometry is 1:1:1:2, x * 157000 + x * 148000 + x * 87000 + 2 * x * 45000, SDS-PAGE
16000
-
x * 210000 + x * 150000 + x * 40000 + x * 34000 + x * 33000 + x * 25000 + x * 20000 + x * 16000 + x * 15000 + x * 13500 + x * 13000, the enzyme contains more than eleven polypeptides, SDS-PAGE
160000
-
betax,beta,sigma,alpha, x * 160000 + x * 145000 + x * 85000 + x * 40000, SDS-PAGE
161000
-
x * 161000 + x * 134000 + x * 72000 + x * 41000 + x * 91000, SDS-PAGE
17500
-
1 * 122000 + 1 * 101000 + 1 * 44000 + 1 * 32000 + 1 * 24000 + 1 * 17500 + 1 * 13800 + 4 * 11800 + 1 * 11200 + 1 * 10800, SDS-PAGE
184000
-
beta,beta,sigma,alpha occur with a stoichiometric ratio of 1:1:1:2, x * 184000 + x * 141000 + x * 55000 + x * 45000, SDS-PAGE
185000
-
x * 185000 + x * 125000 + x * 47000 + x * 30000 + x * 93000, SDS-PAGE
190000
-
x * 190000 + x * 145000 + x * 72000 + x * 38000, SDS-PAGE
20000
-
x * 210000 + x * 150000 + x * 40000 + x * 34000 + x * 33000 + x * 25000 + x * 20000 + x * 16000 + x * 15000 + x * 13500 + x * 13000, the enzyme contains more than eleven polypeptides, SDS-PAGE
20103
-
x * 25608, RpoE2, sequence calculation, x * 20103, RpoE3, sequence calculation
20470
subunit E, calculated from sequence
210000
-
x * 210000 + x * 150000 + x * 40000 + x * 34000 + x * 33000 + x * 25000 + x * 20000 + x * 16000 + x * 15000 + x * 13500 + x * 13000, the enzyme contains more than eleven polypeptides, SDS-PAGE
24000
-
1 * 122000 + 1 * 101000 + 1 * 44000 + 1 * 32000 + 1 * 24000 + 1 * 17500 + 1 * 13800 + 4 * 11800 + 1 * 11200 + 1 * 10800, SDS-PAGE
25000
-
x * 210000 + x * 150000 + x * 40000 + x * 34000 + x * 33000 + x * 25000 + x * 20000 + x * 16000 + x * 15000 + x * 13500 + x * 13000, the enzyme contains more than eleven polypeptides, SDS-PAGE
25608
-
x * 25608, RpoE2, sequence calculation, x * 20103, RpoE3, sequence calculation
32000
-
1 * 122000 + 1 * 101000 + 1 * 44000 + 1 * 32000 + 1 * 24000 + 1 * 17500 + 1 * 13800 + 4 * 11800 + 1 * 11200 + 1 * 10800, SDS-PAGE
33000
-
x * 210000 + x * 150000 + x * 40000 + x * 34000 + x * 33000 + x * 25000 + x * 20000 + x * 16000 + x * 15000 + x * 13500 + x * 13000, the enzyme contains more than eleven polypeptides, SDS-PAGE
34000
-
x * 210000 + x * 150000 + x * 40000 + x * 34000 + x * 33000 + x * 25000 + x * 20000 + x * 16000 + x * 15000 + x * 13500 + x * 13000, the enzyme contains more than eleven polypeptides, SDS-PAGE
34500
-
betax,betax,sigmax,alphax, x * 148000 + x * 142000 + x * 85000 + x * 34500, SDS-PAGE
35000
-
x * 120000 + x * 110000 + x * 95000 + x * 84000 + x * 81000 + x * 75000 + x * 54000 + x * 51000 + x * 42000 + x * 35000, the 110000 Da polypeptide binds nucleoside triphosphates, the 42000 Da polypeptide cross-reacts with antiserum raised to the plastid endoded rpoA gene product, SDS-PAGE
38000
-
x * 190000 + x * 145000 + x * 72000 + x * 38000, SDS-PAGE
40600
enzyme D/L subcomplex, gel filtration
44000
-
1 * 122000 + 1 * 101000 + 1 * 44000 + 1 * 32000 + 1 * 24000 + 1 * 17500 + 1 * 13800 + 4 * 11800 + 1 * 11200 + 1 * 10800, SDS-PAGE
469000
-
core protein of Pol II
47000
-
x * 185000 + x * 125000 + x * 47000 + x * 30000 + x * 93000, SDS-PAGE
500000
-
RNAP I and RNAP II, gel filtration
51000
-
x * 120000 + x * 110000 + x * 95000 + x * 84000 + x * 81000 + x * 75000 + x * 54000 + x * 51000 + x * 42000 + x * 35000, the 110000 Da polypeptide binds nucleoside triphosphates, the 42000 Da polypeptide cross-reacts with antiserum raised to the plastid endoded rpoA gene product, SDS-PAGE
512000
-
holoenzyme complex of Pol II
54000
-
x * 120000 + x * 110000 + x * 95000 + x * 84000 + x * 81000 + x * 75000 + x * 54000 + x * 51000 + x * 42000 + x * 35000, the 110000 Da polypeptide binds nucleoside triphosphates, the 42000 Da polypeptide cross-reacts with antiserum raised to the plastid endoded rpoA gene product, SDS-PAGE
562000
-
non-denaturing gel filtration
60000
-
betax,betax,alphax,sigmax,sigmax, x * 170000 + x * 140000 + x * 40000 + x * 90000 + x * 60000, SDS-PAGE
600000 - 700000
-
RNAP III, gel filtration
75000
-
x * 120000 + x * 110000 + x * 95000 + x * 84000 + x * 81000 + x * 75000 + x * 54000 + x * 51000 + x * 42000 + x * 35000, the 110000 Da polypeptide binds nucleoside triphosphates, the 42000 Da polypeptide cross-reacts with antiserum raised to the plastid endoded rpoA gene product, SDS-PAGE
81000
-
x * 120000 + x * 110000 + x * 95000 + x * 84000 + x * 81000 + x * 75000 + x * 54000 + x * 51000 + x * 42000 + x * 35000, the 110000 Da polypeptide binds nucleoside triphosphates, the 42000 Da polypeptide cross-reacts with antiserum raised to the plastid endoded rpoA gene product, SDS-PAGE
84000
-
x * 120000 + x * 110000 + x * 95000 + x * 84000 + x * 81000 + x * 75000 + x * 54000 + x * 51000 + x * 42000 + x * 35000, the 110000 Da polypeptide binds nucleoside triphosphates, the 42000 Da polypeptide cross-reacts with antiserum raised to the plastid endoded rpoA gene product, SDS-PAGE
90000
-
betax,betax,alphax,sigmax,sigmax, x * 170000 + x * 140000 + x * 40000 + x * 90000 + x * 60000, SDS-PAGE
91000
-
x * 161000 + x * 134000 + x * 72000 + x * 41000 + x * 91000, SDS-PAGE
92000
-
betax,betax,alpha,x,sigmax, x * 140000 + x * 170000 + x * 40000 + x * 92000, SDS-PAGE
93000
-
x * 185000 + x * 125000 + x * 47000 + x * 30000 + x * 93000, SDS-PAGE
9460
x * 9460, calculated from sequence
95000
-
x * 120000 + x * 110000 + x * 95000 + x * 84000 + x * 81000 + x * 75000 + x * 54000 + x * 51000 + x * 42000 + x * 35000, the 110000 Da polypeptide binds nucleoside triphosphates, the 42000 Da polypeptide cross-reacts with antiserum raised to the plastid endoded rpoA gene product, SDS-PAGE
99000
-
x * 99000, T7 polymerase-like structure
100000
Vectrevirus K1E
1 * 100000, SDS-PAGE
100000
x * 100000, SDS-PAGE
124000
-
x * 171000 + x * 124000 + x * 66000 + x * 52000 + x * 41000, SDS-PAGE
124000
-
x * 171000 + x * 124000 + x * 66000 + x * 52000 + x * 41000, SDS-PAGE
124000
-
x * 171000 + x * 124000 + x * 66000 + x * 52000 + x * 41000, SDS-PAGE
124000
-
x * 171000 + x * 124000 + x * 66000 + x * 52000 + x * 41000, SDS-PAGE
140000
-
betax,betax,alphax,sigmax,sigmax, x * 170000 + x * 140000 + x * 40000 + x * 90000 + x * 60000, SDS-PAGE
140000
-
betax,betax,alpha,x,sigmax, x * 140000 + x * 170000 + x * 40000 + x * 92000, SDS-PAGE
140000
-
x * 130000, beta-subunit, plus x * 140000, beta-subunit, SDS-PAGE
145000
-
betax,beta,sigma,alpha, x * 160000 + x * 145000 + x * 85000 + x * 40000, SDS-PAGE
145000
-
x * 190000 + x * 145000 + x * 72000 + x * 38000, SDS-PAGE
148000
-
betax,betax,sigmax,alphax, x * 148000 + x * 142000 + x * 85000 + x * 34500, SDS-PAGE
148000
-
beta,beta,sigma,alpha. Subunit stoichiometry is 1:1:1:2, x * 157000 + x * 148000 + x * 87000 + 2 * x * 45000, SDS-PAGE
151000
-
betax,betax,alphax,sigmax, x * 156000 + x * 151000 + x * 87000 + x * 42000, SDS-PAGE
151000
-
x * 151000 + x * 147000 + x * 55000 + x * 42000, SDS-PAGE
170000
-
betax,betax,alphax,sigmax,sigmax, x * 170000 + x * 140000 + x * 40000 + x * 90000 + x * 60000, SDS-PAGE
170000
-
betax,betax,alpha,x,sigmax, x * 140000 + x * 170000 + x * 40000 + x * 92000, SDS-PAGE
171000
-
x * 171000 + x * 124000 + x * 66000 + x * 52000 + x * 41000, SDS-PAGE
171000
-
x * 171000 + x * 124000 + x * 66000 + x * 52000 + x * 41000, SDS-PAGE
171000
-
x * 171000 + x * 124000 + x * 66000 + x * 52000 + x * 41000, SDS-PAGE
171000
-
x * 171000 + x * 124000 + x * 66000 + x * 52000 + x * 41000, SDS-PAGE
30000
free enzyme, gel filtration
30000
-
x * 185000 + x * 125000 + x * 47000 + x * 30000 + x * 93000, SDS-PAGE
40000
-
x * 210000 + x * 150000 + x * 40000 + x * 34000 + x * 33000 + x * 25000 + x * 20000 + x * 16000 + x * 15000 + x * 13500 + x * 13000, the enzyme contains more than eleven polypeptides, SDS-PAGE
40000
-
betax,betax,alphax,sigmax,sigmax, x * 170000 + x * 140000 + x * 40000 + x * 90000 + x * 60000, SDS-PAGE
40000
-
betax,beta,sigma,alpha, x * 160000 + x * 145000 + x * 85000 + x * 40000, SDS-PAGE
40000
-
x * 146000, beta and beta comigrate, + x * 105000, main sigma factor, + x * 40000, alpha, SDS-PAGE
40000
-
betax,betax,alpha,x,sigmax, x * 140000 + x * 170000 + x * 40000 + x * 92000, SDS-PAGE
41000
-
x * 171000 + x * 124000 + x * 66000 + x * 52000 + x * 41000, SDS-PAGE
41000
-
x * 171000 + x * 124000 + x * 66000 + x * 52000 + x * 41000, SDS-PAGE
41000
-
x * 171000 + x * 124000 + x * 66000 + x * 52000 + x * 41000, SDS-PAGE
41000
-
x * 171000 + x * 124000 + x * 66000 + x * 52000 + x * 41000, SDS-PAGE
41000
-
x * 161000 + x * 134000 + x * 72000 + x * 41000 + x * 91000, SDS-PAGE
42000
-
betax,betax,alphax,sigmax, x * 156000 + x * 151000 + x * 87000 + x * 42000, SDS-PAGE
42000
-
x * 120000 + x * 110000 + x * 95000 + x * 84000 + x * 81000 + x * 75000 + x * 54000 + x * 51000 + x * 42000 + x * 35000, the 110000 Da polypeptide binds nucleoside triphosphates, the 42000 Da polypeptide cross-reacts with antiserum raised to the plastid endoded rpoA gene product, SDS-PAGE
42000
-
x * 151000 + x * 147000 + x * 55000 + x * 42000, SDS-PAGE
45000
-
beta,beta,sigma,alpha occur with a stoichiometric ratio of 1:1:1:2, x * 184000 + x * 141000 + x * 55000 + x * 45000, SDS-PAGE
45000
-
beta,beta,sigma,alpha. Subunit stoichiometry is 1:1:1:2, x * 157000 + x * 148000 + x * 87000 + 2 * x * 45000, SDS-PAGE
480000
-
glycerol gradient centrifugation
52000
-
x * 171000 + x * 124000 + x * 66000 + x * 52000 + x * 41000, SDS-PAGE
52000
-
x * 171000 + x * 124000 + x * 66000 + x * 52000 + x * 41000, SDS-PAGE
52000
-
x * 171000 + x * 124000 + x * 66000 + x * 52000 + x * 41000, SDS-PAGE
52000
-
x * 171000 + x * 124000 + x * 66000 + x * 52000 + x * 41000, SDS-PAGE
55000
-
beta,beta,sigma,alpha occur with a stoichiometric ratio of 1:1:1:2, x * 184000 + x * 141000 + x * 55000 + x * 45000, SDS-PAGE
55000
-
x * 151000 + x * 147000 + x * 55000 + x * 42000, SDS-PAGE
66000
-
x * 171000 + x * 124000 + x * 66000 + x * 52000 + x * 41000, SDS-PAGE
66000
-
x * 171000 + x * 124000 + x * 66000 + x * 52000 + x * 41000, SDS-PAGE
66000
-
x * 171000 + x * 124000 + x * 66000 + x * 52000 + x * 41000, SDS-PAGE
66000
-
x * 171000 + x * 124000 + x * 66000 + x * 52000 + x * 41000, SDS-PAGE
72000
-
x * 161000 + x * 134000 + x * 72000 + x * 41000 + x * 91000, SDS-PAGE
72000
-
x * 190000 + x * 145000 + x * 72000 + x * 38000, SDS-PAGE
85000
-
betax,betax,sigmax,alphax, x * 148000 + x * 142000 + x * 85000 + x * 34500, SDS-PAGE
85000
-
betax,beta,sigma,alpha, x * 160000 + x * 145000 + x * 85000 + x * 40000, SDS-PAGE
87000
-
betax,betax,alphax,sigmax, x * 156000 + x * 151000 + x * 87000 + x * 42000, SDS-PAGE
87000
-
beta,beta,sigma,alpha. Subunit stoichiometry is 1:1:1:2, x * 157000 + x * 148000 + x * 87000 + 2 * x * 45000, SDS-PAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
heterotrimer
-
the three subunits, PB1, PB2 and PA, are all required for both transcription and replication, PB1 carries the polymerase active site, PB2 includes the capped-RNA recognition domain, and PA, whose C-terminal domain consists of 13 alpha-helices and 9 beta-strands, is involved in assembly of the functional complex. The subunit interface is important for virla replication, overview
pentamer
-
subunits structure alpha2betabeta'sigmaomega
?
-
x * 171000 + x * 124000 + x * 66000 + x * 52000 + x * 41000, SDS-PAGE
?
-
x * 185000 + x * 125000 + x * 47000 + x * 30000 + x * 93000, SDS-PAGE
?
-
x * 171000 + x * 124000 + x * 66000 + x * 52000 + x * 41000, SDS-PAGE
?
-
betax,beta,sigma,alpha, x * 160000 + x * 145000 + x * 85000 + x * 40000, SDS-PAGE
?
-
the most probably subunit structure for the enzyme is the following: 154000 + 104000 + 77000 + 64000 + 52000 + 48000 + 46000 + 45000 + 39000
?
-
the most probably subunit structure for the enzyme is the following: 154000 + 104000 + 77000 + 64000 + 52000 + 48000 + 46000 + 45000 + 39000
-
?
-
x * 171000 + x * 124000 + x * 66000 + x * 52000 + x * 41000, SDS-PAGE
?
-
x * 161000 + x * 134000 + x * 72000 + x * 41000 + x * 91000, SDS-PAGE
?
-
x * 99000, T7 polymerase-like structure
?
-
x * 120000 + x * 110000 + x * 95000 + x * 84000 + x * 81000 + x * 75000 + x * 54000 + x * 51000 + x * 42000 + x * 35000, the 110000 Da polypeptide binds nucleoside triphosphates, the 42000 Da polypeptide cross-reacts with antiserum raised to the plastid endoded rpoA gene product, SDS-PAGE
?
-
betax,betax,alphax,sigmax, x * 156000 + x * 151000 + x * 87000 + x * 42000, SDS-PAGE
?
-
betax,betax,alphax,sigmax, x * 156000 + x * 151000 + x * 87000 + x * 42000, SDS-PAGE
-
?
-
betax,betax,sigmax,alphax, x * 148000 + x * 142000 + x * 85000 + x * 34500, SDS-PAGE
?
-
x * 210000 + x * 150000 + x * 40000 + x * 34000 + x * 33000 + x * 25000 + x * 20000 + x * 16000 + x * 15000 + x * 13500 + x * 13000, the enzyme contains more than eleven polypeptides, SDS-PAGE
?
-
x * 25608, RpoE2, sequence calculation, x * 20103, RpoE3, sequence calculation
?
-
x * 25608, RpoE2, sequence calculation, x * 20103, RpoE3, sequence calculation
-
?
-
x * 151000 + x * 147000 + x * 55000 + x * 42000, SDS-PAGE
?
-
x * 146000, beta and beta comigrate, + x * 105000, main sigma factor, + x * 40000, alpha, SDS-PAGE
?
x * 9460, calculated from sequence
?
-
x * 100000, SDS-PAGE
-
?
-
x * 9460, calculated from sequence
-
?
-
x * 171000 + x * 124000 + x * 66000 + x * 52000 + x * 41000, SDS-PAGE
?
-
x * 190000 + x * 145000 + x * 72000 + x * 38000, SDS-PAGE
?
-
beta,beta,sigma,alpha occur with a stoichiometric ratio of 1:1:1:2, x * 184000 + x * 141000 + x * 55000 + x * 45000, SDS-PAGE
?
-
betax,betax,alphax,sigmax,sigmax, x * 170000 + x * 140000 + x * 40000 + x * 90000 + x * 60000, SDS-PAGE
?
-
betax,betax,alpha,x,sigmax, x * 140000 + x * 170000 + x * 40000 + x * 92000, SDS-PAGE
?
-
betax,betax,alpha,x,sigmax, x * 140000 + x * 170000 + x * 40000 + x * 92000, SDS-PAGE
-
?
-
betax,betax,alphax,sigmax,sigmax, x * 170000 + x * 140000 + x * 40000 + x * 90000 + x * 60000, SDS-PAGE
-
decamer
-
core protein of Pol II
decamer
-
1 * 122000 + 1 * 101000 + 1 * 44000 + 1 * 32000 + 1 * 24000 + 1 * 17500 + 1 * 13800 + 4 * 11800 + 1 * 11200 + 1 * 10800, SDS-PAGE
dodecamer
-
holoenzyme complex of Pol II
dodecamer
-
the Rpb2 subunit of RNAP II combines with the Rpb1 subunit to form the RNAP II active site. RNAP II is isolated as a 12 subunit enzyme, Rpb1-Rpb12
dodecamer
-
the Rpb2 subunit of RNAP II combines with the Rpb1 subunit to form the RNAP II active site. RNAP II is isolated as a 12 subunit enzyme, Rpb1-Rpb12
-
monomer
-
-
monomer
-
the enzyme consists of three distinct regions, a catalytic C-terminal polymerase domain (residues 648-1230), an N-terminal domain (residues 369-647) and an N-terminal extension (residues 1-368), domain architecture, overview. The POLRMT C-terminal domain is characteristic of the Pol I family of nucleic acid polymerases, typically described as resembling the shape of a cupped right hand, containing the fingers, palm and thumb subdomains. The palm subdomain contains several key structural motifs that are highly conserved among the different classes of nucleic acid polymerases. The N-terminal extension contains the mitochondrial targeting sequence (residues 1-41), a large, flexible region of unknown structure (residues 42-217) and a pentatricopeptide repeat domain (residues 218-368). The pentatricopeptide repeat domain is connected to the N-terminal domain via a short proline-rich linker region that likely functions as a spacer connecting the two domains. The pentatricopeptide repeat domain consists of two tandem PPR motifs, the domnain contains nine alpha-helices of which four comprise the pentatricopeptide repeat motifs
monomer
Vectrevirus K1E
1 * 100000, SDS-PAGE
multimer
-
bacterial RNAP is a multisubunit enzyme and consists of a core polymerase containing the beta, beta' , and two alpha subunits, together with one or more omega subunits, and a dissociable specificity factor sigma
multimer
-
x * 130000, beta-subunit, plus x * 140000, beta'-subunit, SDS-PAGE
multimer
-
bacterial RNAP is a multisubunit enzyme and consists of a core polymerase containing the beta, beta' , and two alpha subunits, together with one or more omega subunits, and a dissociable specificity factor sigma
oligomer
-
the viral RNA polymerase is composed of four proteins: Late Expression Factor-4 (LEF-4), LEF-8, LEF-9, and P47. Associations are observed between LEF-9 and P47, LEF-4 and P47, and LEF-8 and P47. LEF-4 and LEF-8 do not coimmunoprecipitate but coimmunoprecipitated in the presence of P47, suggesting that they do not associate directly. A weak association is observed between LEF-4 and LEF-9. LEF-8, LEF-9, and P47 have the ability to self-associate
oligomer
-
beta',beta,sigma,alpha. Subunit stoichiometry is 1:1:1:2, x * 157000 + x * 148000 + x * 87000 + 2 * x * 45000, SDS-PAGE
oligomer
-
structure and modeling of the multi-subunit enzyme complex, RNAP subunits can be divided into three groups concerned with catalysis, assembly of the catalytic subunits and auxiliary functions, overview. The large A and B subunits are split into two polypeptides, A'/A'' and B''/B' according to size, they harbour the binding sites for substrate NTPs, duplex DNA template and a 9 bp DNA-RNA hybrid, and provide the catalytic centre, including three catalytic aspartic acid residues and two Mg2+ ions
oligomer
-
RNAPII structure and modeling of the multi-subunit enzyme complex, RNAP subunits can be divided into three groups concerned with catalysis, assembly of the catalytic subunits and auxiliary functions, overview
oligomer
-
RNA polymerase III contains seventeen subunits. The Schizosaccharomyces pombe subunits are expressed in Saccharomyces cerevisiae null mutants and tested for growth. Ten core subunits show heterospecific complementation, but the two largest catalytic subunits (Rpc1 and Rpc2) and all five RNA polymerase III-specific subunits (Rpc82, Rpc53, Rpc37, Rpc34 and Rpc31) are non-functional. Three highly conserved RNA polymerase III-specific domains are found in the twelve-subunit core structure. They correspond to the Rpc17-Rpc25 dimer, involved in transcription initiation, to an N-terminal domain of the largest subunit Rpc1 important to anchor Rpc31, Rpc34 and Rpc82, and to a C-terminal domain of Rpc1 that presumably holds Rpc37, Rpc53 and their Rpc11 partner
oligomer
-
several subunits, e.g. subunit C of 44 kDa
oligomer
-
alpha2betabeta'omega structure and modeling of the multi-subunit enzyme complex, RNAP subunits can be divided into three groups concerned with catalysis, assembly of the catalytic subunits and auxiliary functions, overview
additional information
-
secondary structure and organization of multi-subunit DNA-dependent RNA polymerases, overview. The Rpb8/G RNA polymerase subunit is restricted to eukaryotes and Crenarchaea
additional information
-
secondary structure and organization of multi-subunit DNA-dependent RNA polymerases, overview. The Rpb8/G RNA polymerase subunit is restricted to eukaryotes and Crenarchaea
additional information
-
multi-subunit enzyme
additional information
-
components of the RNA polymerase and their molecular weights determined by SDS-PAGE
additional information
-
components of the RNA polymerase and their molecular weights determined by SDS-PAGE
-
additional information
-
secondary structure and organization of multi-subunit DNA-dependent RNA polymerases, overview. The Rpb8/G RNA polymerase subunit is restricted to eukaryotes and Crenarchaea
additional information
-
dimer-monomer formation is reversible and the equilibrium depends on the ionic strength of the medium. At high ionic strength the enzyme dissociates to a monomeric form
additional information
-
binding of the sigma70 subunit to the core enzyme induces conformational changes in a single-stranded DNA binding region of the protein. As a consequence of these conformational changes, sigma70 subunit gains the specificity for the nontemplate strand of the melted region in the open complex
additional information
-
the core of the procaryotic RNAP comprises five subunits
additional information
-
conformational plasticity of the active center and importance of the bridge helix structure for enzyme activity, overview
additional information
-
secondary structure and organization of multi-subunit DNA-dependent RNA polymerases, overview. The Rpb8/G RNA polymerase subunit is restricted to eukaryotes and Crenarchaea
additional information
-
RNAP contains the vegetative sigma subunit sigma70 (RpoD) and/or the flagellar sigma factor sigma28 (FliA)
additional information
-
existence of two possible conformers: E and E that are in rapid equilibrium. Both forms can form the quarternary complex, but only the E form is capable of catalyzing phosphodiester bond formation
additional information
-
subunits with molecular weights of 60 kDa and 45 kDa and a subunit with a molecular weight of 52 kDa (which is probably one of the basal transcription factors of RNA polymerase III) are modified in the composition of the enzyme isolated from human cells. The three subunits are simultaneously phosphorylated and glycosylated
additional information
the gene locus for the largest subunit is identified and its primary structure is determined
additional information
-
the gene locus for the largest subunit is identified and its primary structure is determined
additional information
-
secondary structure and organization of multi-subunit DNA-dependent RNA polymerases, overview. The Rpb8/G RNA polymerase subunit is restricted to eukaryotes and Crenarchaea. The enzyme lacks the G and M polypeptides
additional information
-
3D structure of the RNA polymerase from the mitochondrial plasmid is T7 polymerase-like, modeling using molecular mechanics and molecular dynamics, overview
additional information
-
subunits with molecular weights of 49 kDa and 42 kDa and a subunit with a molecular weight of 45 kDa (which is probably a component of the basal transcription factor of RNA polymerase III, since it is not identified in the mouse enzyme) are modified in the composition of the enzyme isolated from mouse fibroblasts. The two subunits are simultaneously phosphorylated and glycosylated (glycosylation by O-N-acetylglucosamine residues)
additional information
-
secondary structure and organization of multi-subunit DNA-dependent RNA polymerases, overview. The Rpb8/G RNA polymerase subunit is restricted to eukaryotes and Crenarchaea. The enzyme lacks the G subunit
additional information
-
secondary structure and organization of multi-subunit DNA-dependent RNA polymerases, overview. The Rpb8/G RNA polymerase subunit is restricted to eukaryotes and Crenarchaea
additional information
-
subunit RpoS of RNA polymerase is a central regulator which governs the expression of a host of stationary phase-induced and osmotically regulated genesin gram-negative bacteria.
additional information
-
subunit RpoS of RNA polymerase is a central regulator which governs the expression of a host of stationary phase-induced and osmotically regulated genesin gram-negative bacteria.
-
additional information
-
secondary structure and organization of multi-subunit DNA-dependent RNA polymerases, overview. The Rpb8/G RNA polymerase subunit is restricted to eukaryotes and Crenarchaea
additional information
-
the enzyme lacks the Rpb8 and Rpo13 subunits
additional information
-
structure analysis and modeling, overview
additional information
-
conformational plasticity of the active center and importance of the bridge helix structure for enzyme activity, overview
additional information
-
secondary structure and organization of multi-subunit DNA-dependent RNA polymerases, overview. The Rpb8/G RNA polymerase subunit is restricted to eukaryotes and Crenarchaea. The enzyme lacks the G subunit
additional information
-
structure analysis, overview, the enzyme contains a subunit Rpo13 located at a groove between the H subunit and the clamp head domain of the A' subunit, model ing including the A' subunit jaw and clamp head domains and RpoG and Rpo13, overview
additional information
-
analysis of interaction sbetween the largest subunit Rpb1 and the other subunits, overview
additional information
-
conformational plasticity of the active center and importance of the bridge helix structure for enzyme activity, overview
additional information
-
detailed RNAPII structure study in different comformations, e.g. concerning the trigger loop, using crystal structures, the collective set of all normal modes describes enzyme flexibility as a function of residue in terms of root mean square fluctuations, RMSF values are directly related to crystallographic B-factors, enzyme motions described by individual modes, caclulations, overview
additional information
peptide regions that interact with regulatory factors are close to the Pol II surface and assume seemingly flexible loop structures, one is located in the TFIIF-interacting protrusion domain, the other is located in the TFIIE-interacting clamp domain, conformations, e.g. of the TFIIF-interacting Rpb2 protrusion, overview. Conformational movement and dynamics of fork loop-1 and -2. mechanism, overview
additional information
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secondary structure and organization of multi-subunit DNA-dependent RNA polymerases, overview. The Rpb8/G RNA polymerase subunit is restricted to eukaryotes and Crenarchaea
additional information
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the enzyme consists of three distinct regions, a catalytic C-terminal polymerase domain, an N-terminal domain and an N-terminal extension, a pentatricopeptide repeat domain is not present in the yeast enzyme
additional information
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the C-terminal domain (CTD) of RNA polymerase II in eukaryotes is comprised of tandemly repeating units of a conserved seven-amino acid sequence. DNA instability may play a role in regulating or maintaining C-terminal domain repeat number. 36 diverse Saccharomyces cerevisiae isolates reveal evidence of numerous past rearrangements within the DNA sequence that encodes the C-terminal domain, the total number of CTD repeats is relatively static (24-26 repeats in all strains), suggesting a balancing act between repeat expansion and contraction. Presence of DNA secondary structures, specifically G-quadruplex-like DNA,within the CTD coding region. Mutating PIF1, a G-quadruplex-specific helicase, results in increased CTD repeat length polymorphisms. RAD52 is necessary for CTD repeat expansion but not contraction, identifying a role for recombination in repeat expansion
additional information
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the C-terminal domain (CTD) of RNA polymerase II in eukaryotes is comprised of tandemly repeating units of a conserved seven-amino acid sequence. DNA instability may play a role in regulating or maintaining C-terminal domain repeat number. 36 diverse Saccharomyces cerevisiae isolates reveal evidence of numerous past rearrangements within the DNA sequence that encodes the C-terminal domain, the total number of CTD repeats is relatively static (24-26 repeats in all strains), suggesting a balancing act between repeat expansion and contraction. Presence of DNA secondary structures, specifically G-quadruplex-like DNA,within the CTD coding region. Mutating PIF1, a G-quadruplex-specific helicase, results in increased CTD repeat length polymorphisms. RAD52 is necessary for CTD repeat expansion but not contraction, identifying a role for recombination in repeat expansion
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additional information
enzyme structure analysis and comparison to the structures of Saccharomyces cerevisiae and human Pol IIs, overview
additional information
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enzyme structure analysis and comparison to the structures of Saccharomyces cerevisiae and human Pol IIs, overview
additional information
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at 0.5 M NH4CI the enzyme exists in the monomeric form
additional information
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peptide and subunit mapping for determination of the substrate binding site
additional information
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secondary structure and organization of multi-subunit DNA-dependent RNA polymerases, overview. The Rpb8/G RNA polymerase subunit is restricted to eukaryotes and Crenarchaea
additional information
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components of the RNA polymerase and their molecular weights determined by SDS-PAGE
additional information
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components of the RNA polymerase and their molecular weights determined by SDS-PAGE
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additional information
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secondary structure and organization of multi-subunit DNA-dependent RNA polymerases, overview. The Rpb8/G RNA polymerase subunit is restricted to eukaryotes and Crenarchaea
additional information
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components of the RNA polymerase and their molecular weights determined by SDS-PAGE
additional information
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components of the RNA polymerase and their molecular weights determined by SDS-PAGE
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additional information
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conformational plasticity of the active center and importance of the bridge helix structure for enzyme activity, overview
additional information
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the bacterial RNAP uses a homodimeric assembly platform
additional information
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conformational plasticity of the active center and importance of the bridge helix structure for enzyme activity, overview
additional information
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subunits RPB5 and RPB6 localize to discrete subnuclear compartments and form part of different polymerase complexes. RNA interference mediated depletion of these discrete subunits abolishes class-specific transcription
additional information
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the PSi-C-terminal domain of large subunit RPB1 is essential for cell survivial and production of both SL RNA and mRNA, the Trypanosoma brucei enzyme lacks conserved heptapeptide sequence motifs found in most other eukaryotes
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C70A/C72H/C85A/C88H
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mutant enzyme is defective in intrinsic termination and antitermination in vitro. Mutation likely causes a recessive-lethal phenotype
C70H
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mutant enzyme terminates more poorly than wild-type enzyme on put(-) templates, and responds weakly on put. Mutation likely causes a recessive-lethal phenotype
C72H
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mutant enzyme terminates more poorly than wild-type enzyme on put(-) templates, and responds weakly on put. Mutation likely causes a recessive-lethal phenotype
C85H
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mutant enzyme terminates more poorly than wild-type enzyme on put(-) templates, and responds weakly on put. Mutation likely causes a recessive-lethal phenotype
del70-88insGGGG
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mutant enzyme terminates more poorly than wild-type enzyme on put(-) templates, and responds weakly on put. Mutation likely causes a recessive-lethal phenotype
del74-84insGGGG
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mutant enzyme terminates more poorly than wild-type enzyme on put(-) templates, and responds weakly on put. Mutation likely causes a recessive-lethal phenotype
E813A/D814A
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significantly decreased elongation rate, the mutation changes the effect of diphosphate on the 3'-5'-exonuclease reaction, whose addition stimulates the production of UMP through hydrolysis rather than of UTP through diphosphorolysis. The mutation makes the 3'-exonuclease activity independent of TTP. The mutation changes the response of TEC to diphosphate: instead of causing diphosphorolysis it stimulates the exonuclease reaction
N458A
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significantly decreased elongation rate
R1106A
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significantly decreased elongation rate, enhanced exonuclease activity
E244stop
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random mutagenesis, identification of mutant L33, a truncated protein that lacks the C-terminal alpha-subunit, alphaCTD, but is capable of being assembled into the RNAP and carrying out transcription, while it does not respond to signals in the DNA or from protein effectors, overview. The mutant grows faster and exhibits a higher accumulated cell mass than the wild-type in the presence of butanol, phenotype, overview
V257F/L281P
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random mutagenesis, the rpoA14 mutant shows mutations of the C-terminal alpha-subunit, phenotype, overview
V257R
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random mutagenesis, the rpoA22 mutant shows a mutation of the C-terminal alpha-subunit, phenotype, overview
D421A
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mutation results in an enzyme with reduced activity and altered patterns of transcription
D421T
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mutation results in an enzyme with reduced activity and altered patterns of transcription
K631R
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the fraction of catalytically active E form is 38% compared to 100% for the wild-type enzyme. The synthesis of long transcripts is markedly diminished for the mutant due to decreasing processivity
R423A
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mutation results in an enzyme with reduced activity and altered patterns of transcription
R423K
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mutation results in an enzyme with reduced activity and altered patterns of transcription
R425K
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mutation results in an enzyme with reduced activity and altered patterns of transcription
S641A
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mutation reduces activity in presence of Mg2+ to 93% of the activity of the wild-type enzyme
W422A
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mutation results in an enzyme that has nearly normal levels of activity and exhibits patterns of transcription that are similar to that of the wild-type enzyme
W422F
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mutation results in an enzyme that has nearly normal levels of activity and exhibits patterns of transcription that are similar to that of the wild-type enzyme
W422R
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mutation results in an enzyme that has nearly normal levels of activity and exhibits patterns of transcription that are similar to that of the wild-type enzyme
W422S
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mutation results in an enzyme that has nearly normal levels of activity and exhibitspatterns of transcription that arew similar to that of the wild-type enzyme
Y639/S641A
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mutation reduces activity in presence of Mg2+ to 89% of the activity of the wild-type enzyme
Y639C
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mutation reduces activity in presence of Mg2+ to 7.5% of the activity of the wild-type enzyme. The mutation reduces the catalytic specificity for ribonucleoside triphosphates versus deoxynucleoside triphosphates during transcript elongation, which is about 80 for the wild-type enzyme. The remaining specificity factor is 11
Y639H
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mutation reduces activity in presence of Mg2+ to 3.7% of the activity of the wild-type enzyme
Y639L
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mutation reduces activity in presence of Mg2+ to 43% of the activity of the wild-type enzyme. The mutation reduces the catalytic specificity for ribonucleoside triphosphates versus deoxynucleoside triphosphates during transcript elongation, which is about 80 for the wild-type enzyme. The remaining specificity factor is 11
Y639M
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mutation reduces activity in presence of Mg2+ to 50% of the activity of the wild-type enzyme. The mutation reduces the catalytic specificity for ribonucleoside triphosphates versus deoxynucleoside triphosphates during transcript elongation, which is about 80 for the wild-type enzyme. The remaining specificity factor is 5.5
Y639Q
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mutation reduces activity in presence of Mg2+ to 1% of the activity of the wild-type enzyme. The mutation reduces the catalytic specificity for ribonucleoside triphosphates vs deoxynucleoside triphosphates during transcript elongation, which is about 80 for the wild-type enzyme. The remaining specificity factor is 4.5
Y639T
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mutation reduces activity in presence of Mg2+ to 1.3% of the activity of the wild-type enzyme. The mutation reduces the catalytic specificity for ribonucleoside triphosphates versus deoxynucleoside triphosphates during transcript elongation, which is about 80 for the wild-type enzyme. The remaining specificity factor is 6.5
Y639V
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mutation reduces activity in presence of Mg2+ to 4.3% of the activity of the wild-type enzyme. The mutation reduces the catalytic specificity for ribonucleoside triphosphates versus deoxynucleoside triphosphates during transcript elongation, which is about 80 for the wild-type enzyme. The remaining specificity factor is 19
G711K/N926S/N1103S/N1117S
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site-directed mutagenesis, the mutant mitoRNAP that lacks four natural hydroxylamine cleavage sites
L640D
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the mutant of the PA subunit shows reduced transcriptional activity compared to the wild-type enzyme
L666D
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the mutant of the PA subunit shows reduced transcriptional activity compared to the wild-type enzyme
V636S
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the mutant of the PA subunit shows reduced transcriptional activity compared to the wild-type enzyme
W706A
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the mutant of the PA subunit shows reduced transcriptional activity compared to the wild-type enzyme
H426N
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the rpoB(R)-specific missense mutation is essential for the activation of secondary metabolism, molecular mechanism, overview
R584A
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site-directed mutagenesis, the RNAP holoenzyme containing this sigma70 mutant binds preferentially to promoters bearing a specifically mutated -35 element
D505A
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mutation in subunit Rpb2, the mutant shows a weak defect in the escape from a transcriptional stall at A20
E1028Q
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mutation in subunit Rpb2, the mutant shows transcription elongation defects
E529Q
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the substitution mutant is are slower than the wild-type enzyme in RNA elongation
G985A/G987A
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the double substitution in subunit Rpb2 is expected to subtly affect the conformation and/or dynamics of K987, an essential residue
K979Q
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lethal mutation in subunit Rpb2
K979R
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lethal mutation in subunit Rpb2
K987Q
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lethal mutation in subunit Rpb2
K987R
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lethal mutation in subunit Rpb2
Q513A
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mutation in subunit Rpb2, the mutant shows a weak defect in the escape from a transcriptional stall at A20
R1020K
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lethal mutation in subunit Rpb2
R1020Q
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lethal mutation in subunit Rpb2
R512A
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mutation in subunit Rpb2, the mutant shows transcription elongation defects
R766A
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the substitution is lethal, consistent with an important role for this invariant latch residue
R766Q
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the substitution is lethal, consistent with an important role for this invariant latch residue
D505A
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mutation in subunit Rpb2, the mutant shows a weak defect in the escape from a transcriptional stall at A20
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E529A
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mutation in subunit Rpb2, the mutant is faster in elongation compared to wild type RNAP II
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E529D
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mutation in subunit Rpb2, the mutant is faster in elongation compared to wild type RNAP II
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R512C
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mutation in subunit Rpb2, the mutant shows transcription elongation defects
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R428A
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site-directed mutagenesis, designed based on substitutions at the homologous position (Rpb2 R512) of Saccharomyces cerevisiae RNAP II, used as a reference structure, molecular dynamics simulations with starting Tt RNAP TEC structure, PDB 205J, that is in a strained, catalytic conformation that responds very sensitively to the R428A substitution but is stable for wild-type enzyme, overview. Long range conformational coupling linking a dynamic segment of the bridge alpha-helix, the extended fork loop, the active site, and the trigger loop-trigger helix is apparent and adversely affected in beta R428A RNAP. The R428A substitution is instable in the i+1 dTMP-ATP base pair, as indicated by fluctuations in the dTMP O4-ATP N6 base pairing distance in R428A
Y639F
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mutation reduces the catalytic specificity for ribonucleoside triphosphates vs deoxynucleoside triphosphates during transcript elongation, which is about 80 for the wild-type enzyme by a factor of 20 and largely eliminates the KM-difference between rNTPs and dNTPs. The remaining specificity factor of 4 is turnover-number-mediated and is nearly eliminated if Mn2+ is substituted for Mg2+ in the reaction. Mn2+ substitution does not significantly affect the Km difference between rNTPs and dNTPs
Y639F
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the fraction of catalytically active E form is 32% compared to 100% for the wild-type enzyme
E529A
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mutation in subunit Rpb2, the mutant is faster in elongation compared to wild type RNAP II
E529A
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the substitution mutant is are faster than the wild-type enzyme in RNA elongation
E529D
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mutation in subunit Rpb2, the mutant is faster in elongation compared to wild type RNAP II
E529D
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the substitution mutant is are faster than the wild-type enzyme in RNA elongation
R512C
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mutation in subunit Rpb2, the mutant shows transcription elongation defects
R512C
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site-directed mutagenesis, the highly conserved residue is located about 20 A from Mg2+-I and just C-terminal to the fork loop, molecular dynamics simulations, overview. Mutant Sc Rpb2 R512C is slow in elongation and shows transcriptional defects. Rpb2 R512C may have a defect in CTP-Mg2+ sequestration
additional information
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RNAP mutants: the N-terminal region of T7 RNAP contains a nascent RNA binding site that functions to retain the nascent chain within the ternary complex. The region surrounding residue 240 is involved in binding the initiating NTP. Residues at the very C terminus of T7 RNAP are involved in binding the elongating NTP
additional information
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combined shRNA and dsRNA POLRMT gene silencing
additional information
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suppression of subunit RPC32alpha expression in HeLa cells by siRNAs. Levels of p53 and lamin A/C are dramatically downregulated by ectopic RPC32alpha expression, but either unchanged (lamin A/C) or moderately increased (p53) by ectopic RPC32beta subunit expression
additional information
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for genetic inhibition of Pol III, A549 cells are transfected with siRNA against POLR3G (siPOLR3G_1 and siPOLR3G_2), a subunit of the Pol III complex, or negative control siRNA
additional information
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phenotypes of several sigma70 mutants and of diverse rsd mutants, genetic screening for isolating enhanced-function Rsd mutants, overview. Interaction of Rsd and AlgQ mutants with region 2 and 4 of sigma70, overview
additional information
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mutagenesis by amino-acid replacements altering the RNA polymerase II Switch 1 loop domain, such as rpb1-L1397S. rpb1-L1397S enhances RNA polymerase II occupancy downstream of the URA2 initiator
additional information
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mutations are made in highly conserved residues Rpb2 K979, K987, and R1020 within the active site region of RNAP II, at positions that potentially might be essential for catalytic function. Mutations are constructed in an extended fork region of subunit Rpb2, residues R504-E529, construction of diverse mutant strains, e.g. strain yBC-9 expressing subunit Rpb2 under the control of the Gal promoter and is deleted for the chromosomal copy of the DST1 gene, encoding transcription factor IIS, TFIIS. From the strain yBC-9, the strain yBC-32 was constructed by transformation with pFL39-RPB2-TAP, TRP1
additional information
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mutations are made in highly conserved residues Rpb2 K979, K987, and R1020 within the active site region of RNAP II, at positions that potentially might be essential for catalytic function. Mutations are constructed in an extended fork region of subunit Rpb2, residues R504-E529, construction of diverse mutant strains, e.g. strain yBC-9 expressing subunit Rpb2 under the control of the Gal promoter and is deleted for the chromosomal copy of the DST1 gene, encoding transcription factor IIS, TFIIS. From the strain yBC-9, the strain yBC-32 was constructed by transformation with pFL39-RPB2-TAP, TRP1
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additional information
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the enzyme is chemically modified with AMP o-formylphenyl ester followed by reduction with borohydride, the modified protein catalyzes the labeling of its own largest subunit when incubated with [alpha33P]UTP in the presence of poly[d(A-T)], followed by mapping through using cyanogen bromide, hydroxylamine, or amino acid-specific endoproteinases, overview
additional information
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simulation of diverse McJ25-resistant mutations and their effects on enzyme activity, overview
additional information
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RNAi-targeting of mRNA 39UTR allows regulated depletion of RPB1, mutant RNAP-II containing 1/3 Psi-C-terminal domain is defective in transcription and causes abortive initiation, it is toxic and causes cell death, while a 2/3 Psi-C-terminal domain mutant maintains steady-state transcript levels and still supports cell growth,, overview
additional information
recombinant Xcc core RNAP lacking omega shows a 13fold decrease in enzymatic activity in comparison with that containing omega. Promoter-specific transcription assays by recombinant Xcc core RNAP reconstituted with external added sigma factor show that the absence of omega debilitates the transcriptional activity of Xcc RNAP
additional information
recombinant Xcc core RNAP lacking omega shows a 13fold decrease in enzymatic activity in comparison with that containing omega. Promoter-specific transcription assays by recombinant Xcc core RNAP reconstituted with external added sigma factor show that the absence of omega debilitates the transcriptional activity of Xcc RNAP
additional information
recombinant Xcc core RNAP lacking omega shows a 13fold decrease in enzymatic activity in comparison with that containing omega. Promoter-specific transcription assays by recombinant Xcc core RNAP reconstituted with external added sigma factor show that the absence of omega debilitates the transcriptional activity of Xcc RNAP
additional information
recombinant Xcc core RNAP lacking omega shows a 13fold decrease in enzymatic activity in comparison with that containing omega. Promoter-specific transcription assays by recombinant Xcc core RNAP reconstituted with external added sigma factor show that the absence of omega debilitates the transcriptional activity of Xcc RNAP
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C-terminal domain encoding DNA and amino acid sequence determination and analysis, genotyping, sequence comparisons of the CTD region from 36 yeast strains. The DNA helicase Pif1 suppresses CTD rearrangement
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cloning of the cDNA for the mtRNAP of Physarum and expression in Escherichia coli
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cloning of the genes for the three large subunits A, B and C, which are organized in line in the order B-A-C, genetic organization, DNA and amino acid sequence determination and anaylsis, the three RNA polymerase subunit genes are cotranscribed together with an ORF of 88 amino acid residues length situated immediately upstream of the B gene and two ORFs of 104 and 130 amino acid residues following the C gene, overview
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construction of plasmids with polylinker cloning sites adjacent to the RNA polymerase promoter
expressed in Escherichia coli as an N-terminal maltose binding protein (MBP) fusion protein
expressed in HEK-293T cells, HAT-1080 cells, and Magi cells
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expression in a phage display using Halobacterium phage phi H, method overview
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expression in Escherichia coli
expression in Saccharomyces cerevisiae
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expression of C-terminally His-tagged alpha subunit-encoded by gene rpoA, and coexpression of the subunits of Xanthomonas campestris pv. campestris core RNAP from plasmid pBBad22K in Escherichia coli strain BL21(DE3), overexpression with or without omega
expression of His-tagged subunits PA and PB1 in Escherichia coli
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expression of the N-terminally His6-tagged intein fusion mitoRNAP protein
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expression of the T7 RNA polymerase tagged with yellow fluorescent protein and His6 in Rhodobacter capsulatus strain B10S establishing an additional expression system for the enzyme, method optimization and system evaluation, comparison to the Escherichia coli strain BL21(DE3) expression system, both using the expression vector pRhotHi-2-yfp-His6, overview. T7 RNA polymerase subcloning in Escherichia coli strain DH5alpha. Quantitative expression analysis, overview
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gene k1ep, expression of His6-tagged K1E in Escherichia coli strain bL21(DE3), recombinant expression of K1E RNA polymerase in Bacillus megaterium strain MS941, a nprM deletion mutant of DSM319, using K1E promoters or SP6 promoter and a PEG-mediated transformation, method development and evaluation. The T7 RNAP promoter is not recognized at all
Vectrevirus K1E
gene rpoA, library screening
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gene rpoA, recombinant expression of the C-terminally His9-tagged enzyme in Escherichia coli B834 (DE3) cells, subcloning in Escherichia coli strain DH5alpha
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gene rpoA, recombinant expression of the HA-tagged alpha-subunit in transplastomic tobacco plants, analysis of the distribution of the tagged polymerase in plastid subfractions, and associated genes are identified under various light conditions. RpoA:HA is detected as early as the 3rd day after imbibition, and is constitutively expressed in green tissue over 60 days of plant development. Phenotypes of tagged RpoA and wild-type control lines, overview. Transplastomic tobacco plants grown on soil are phenotypically indistinguishable from wild-type
gene rpoB encodes the RNA polymerase beta subunit, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis of rpoB
gene rpoB, encoding the beta subunit of the DNA-directed RNA polymerase of phytoplasma, genetic structure, genotyping and phylogenetic analysis, detailed overview
gene rpoT, single copy gene, DNA and amino acid sequence determination and analysis, sequence comparisons, genetic structure and phylogenetic analysis, N-terminal transit peptide of SmRpoT confers targeting of green fluorescent-tagged protein exclusively to mitochondria after transient expression in Arabidopsis thaliana and Selaginella moellendorffii protoplasts
gene TON-0309 encoding DNA-directed RNA polymerase subunit L, recombinant overexpression of subunit L in Escherichia coli strain BL21(DE3)
genes encoding subunits of the enzyme, DNA and amino acid sequence determination and analysis, genetic organization involving the genes of the transcription machinery, i.e. gene tfis
genes for the subunits beta and beta
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genes rpoA, rpoB, rpoC1, and rpoC2 encoding the enzyme subunits, DNA and amino acid sequence determination and analysis, phylogenetic analysis, number of sites containing synonymous and nonsynonymous substitutions, overview
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genes rpoE2 and rpoE3, phage library screening, DNA and amino acid sequence determination and analysis, genetic organization and associated sigma factors, phylogenetic analysis of the sigma factors, overview
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identification and sequencing of the SK7 promoter, sequence comparison of the porcine SK7 snRNA with sequences from other organisms, overview
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isolation and characterisation of a cDNA encoding the RNA polymerase common subunit RPB6
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mitochondrial plasmid sequence determination and analysis, the viral-like RNA polymerase ORF has 3' and 5' inverted terminal repeats, also a 5' binding protein. This protein can be involved in both replication and integration processes of these plasmid in the mitochondrial genome
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overexpression of His6-tagged subunit D of the RNA polymerase. A shuttle expression vector system for Pyrococcus furiosus and Escherichia coli is described allowing the regulated expression of proteins in Pyrococcus. A shuttle vector of Pyrococcus abyssi is redesigned using the overexpression of the HMG-CoA reductase as a selection marker which confers resistance to the antibiotic simvastatin
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Production of different translational and transcriptional fusions in Escherichia coli. PCR fragments of different sizes are cloned into plasmids resulting in intermediate constructs.
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recombinant expression of wild-type ProtA-tagged enzyme PolI in strain y2423. The second largest subunit of one polymerase is expressed as a C-terminal fusion protein with a protein A tag. Between the C terminus of the subunit and the protein A part, a recognition site for TEV protease is located
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recombinant Rpb2 R512C, TAP-tagged at the C-terminus of the RNAP II Rpb9 subunit
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RNAPsubunit 2, RNAP2, DNA and amino acid sequence determination and analysis, detailed phylogenetic analysis and tree. Reconstruction of putative ancestral RNAP2 from the genome of eukaryote Hydra magnipapillata and Phytophthora parasitica using viral RNAP2, detection of megaviruse DNAs that are integrated into eukaryote genomes and misclassified
RPB2 gene encoding the Rpb2 subunit of yeast RNAP II, expression of mutant enzyme and subunits in Escherichia coli strain XL-1 Blue
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rpoB(R) markedly activates antibiotic biosynthesis in the wild-type Streptomyces lividans strain 1326 and also in strain KO-421, a relaxed mutant unable to produce ppGpp, phenotypes, overview
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stable ectopic expression of subunit RPC32alpha in IMR90 fibroblasts
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the genes for the large subunits beta and beta are cloned and sequenced. MW for beta and beta, calculated from nucleotide sequence is 190522 Da and 143139 Da
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the genes rpoA, rpoB and rpoC which encode the RNA polymerase, alpha-, beta- and betasubunits, respectively, have been individually placed on expression plasmids under control of the bacteriophage T7 promoter. Induction of the T7 RNA polymerase gene in hist cells harbouring each of the three plasmids, results in the extensive overproduction of the three polypeptides
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construction of plasmids with polylinker cloning sites adjacent to the RNA polymerase promoter
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construction of plasmids with polylinker cloning sites adjacent to the RNA polymerase promoter
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construction of plasmids with polylinker cloning sites adjacent to the RNA polymerase promoter
Zindervirus SP6
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expression in Escherichia coli
expression in Escherichia coli
gene rpoB encodes the RNA polymerase beta subunit, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis of rpoB
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gene rpoB encodes the RNA polymerase beta subunit, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis of rpoB
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gene rpoB encodes the RNA polymerase beta subunit, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis of rpoB
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gene rpoB encodes the RNA polymerase beta subunit, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis of rpoB
gene rpoB encodes the RNA polymerase beta subunit, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis of rpoB
gene rpoB encodes the RNA polymerase beta subunit, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis of rpoB
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gene rpoB encodes the RNA polymerase beta subunit, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis of rpoB
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gene rpoB encodes the RNA polymerase beta subunit, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis of rpoB
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gene rpoB encodes the RNA polymerase beta subunit, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis of rpoB
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gene rpoB encodes the RNA polymerase beta subunit, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis of rpoB
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gene rpoB, encoding the beta subunit of the DNA-directed RNA polymerase of phytoplasma, genetic structure, genotyping and phylogenetic analysis, detailed overview
gene rpoB, encoding the beta subunit of the DNA-directed RNA polymerase of phytoplasma, genetic structure, genotyping and phylogenetic analysis, detailed overview
gene rpoB, encoding the beta subunit of the DNA-directed RNA polymerase of phytoplasma, genetic structure, genotyping and phylogenetic analysis, detailed overview
gene rpoB, encoding the beta subunit of the DNA-directed RNA polymerase of phytoplasma, genetic structure, genotyping and phylogenetic analysis, detailed overview
gene rpoB, encoding the beta subunit of the DNA-directed RNA polymerase of phytoplasma, genetic structure, genotyping and phylogenetic analysis, detailed overview
gene rpoB, encoding the beta subunit of the DNA-directed RNA polymerase of phytoplasma, genetic structure, genotyping and phylogenetic analysis, detailed overview
gene rpoB, encoding the beta subunit of the DNA-directed RNA polymerase of phytoplasma, genetic structure, genotyping and phylogenetic analysis, detailed overview
gene rpoB, encoding the beta subunit of the DNA-directed RNA polymerase of phytoplasma, genetic structure, genotyping and phylogenetic analysis, detailed overview
gene rpoB, encoding the beta subunit of the DNA-directed RNA polymerase of phytoplasma, genetic structure, genotyping and phylogenetic analysis, detailed overview
gene rpoB, encoding the beta subunit of the DNA-directed RNA polymerase of phytoplasma, genetic structure, genotyping and phylogenetic analysis, detailed overview
gene rpoB, encoding the beta subunit of the DNA-directed RNA polymerase of phytoplasma, genetic structure, genotyping and phylogenetic analysis, detailed overview
gene rpoB, encoding the beta subunit of the DNA-directed RNA polymerase of phytoplasma, genetic structure, genotyping and phylogenetic analysis, detailed overview
'Gomphocarpus physocarpus' phytoplasma
gene rpoB, encoding the beta subunit of the DNA-directed RNA polymerase of phytoplasma, genetic structure, genotyping and phylogenetic analysis, detailed overview
gene rpoB, encoding the beta subunit of the DNA-directed RNA polymerase of phytoplasma, genetic structure, genotyping and phylogenetic analysis, detailed overview
gene rpoB, encoding the beta subunit of the DNA-directed RNA polymerase of phytoplasma, genetic structure, genotyping and phylogenetic analysis, detailed overview
gene rpoB, encoding the beta subunit of the DNA-directed RNA polymerase of phytoplasma, genetic structure, genotyping and phylogenetic analysis, detailed overview
gene rpoB, encoding the beta subunit of the DNA-directed RNA polymerase of phytoplasma, genetic structure, genotyping and phylogenetic analysis, detailed overview
'Zea mays' phytoplasma
gene rpoB, encoding the beta subunit of the DNA-directed RNA polymerase of phytoplasma, genetic structure, genotyping and phylogenetic analysis, detailed overview
gene rpoB, encoding the beta subunit of the DNA-directed RNA polymerase of phytoplasma, genetic structure, genotyping and phylogenetic analysis, detailed overview
gene rpoB, encoding the beta subunit of the DNA-directed RNA polymerase of phytoplasma, genetic structure, genotyping and phylogenetic analysis, detailed overview
RNAPsubunit 2, RNAP2, DNA and amino acid sequence determination and analysis, detailed phylogenetic analysis and tree. Reconstruction of putative ancestral RNAP2 from the genome of eukaryote Hydra magnipapillata and Phytophthora parasitica using viral RNAP2, detection of megaviruse DNAs that are integrated into eukaryote genomes and misclassified
RNAPsubunit 2, RNAP2, DNA and amino acid sequence determination and analysis, detailed phylogenetic analysis and tree. Reconstruction of putative ancestral RNAP2 from the genome of eukaryote Hydra magnipapillata and Phytophthora parasitica using viral RNAP2, detection of megaviruse DNAs that are integrated into eukaryote genomes and misclassified
R4THW7; R4TFI0
RNAPsubunit 2, RNAP2, DNA and amino acid sequence determination and analysis, detailed phylogenetic analysis and tree. Reconstruction of putative ancestral RNAP2 from the genome of eukaryote Hydra magnipapillata and Phytophthora parasitica using viral RNAP2, detection of megaviruse DNAs that are integrated into eukaryote genomes and misclassified
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