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2.7.7.6: DNA-directed RNA polymerase

This is an abbreviated version!
For detailed information about DNA-directed RNA polymerase, go to the full flat file.

Word Map on EC 2.7.7.6

Reaction

nucleoside triphosphate
+
RNAn
=
diphosphate
 +
RNAn+1

Synonyms

C RNA formation factors, chloroplast soluble RNA polymerase, deoxyribonucleic acid-dependent ribonucleic acid polymerase, DNA-dependent ribonucleate nucleotidyltransferase, DNA-dependent RNA nucleotidyltransferase, DNA-dependent RNA polymerase, DNA-dependent RNA polymerase I, DNA-dependent RNA polymerase III, DNA-dependent RNAP, h-mtRNAP, K1E RNAP, mitochondrial RNA polymerase, mitoRNAP, More, mtRNAP, multi-subunit RNA polymerase, nucleotidyltransferase, ribonucleate, plastid RNA polymerase, plastid-encoded polymerase, plastid-encoded RNA polymerase, Pol I, Pol II, pol III, Pol IIIalpha, Pol IIIbeta, Pol IV, Pol V, polI, PolIII, POLRMT, ribonucleate nucleotidyltransferase, ribonucleate polymerase, ribonucleic acid formation factors, C, ribonucleic acid nucleotidyltransferase, ribonucleic acid polymerase, ribonucleic acid transcriptase, ribonucleic polymerase, ribonucleic transcriptase, rifampicin-resistant RNA polymerase, RNA formation factors, C, RNA nucleotidyltransferase, RNA nucleotidyltransferase (DNA-directed), RNA pol III, RNA polymerase, RNA polymerase core enzyme, RNA polymerase I, RNA polymerase II, RNA polymerase II complex, RNA polymerase III, RNA polymerase III complex, RNA transcriptase, RNAP, RNAP core enzyme, RNAP I, RNAP II, RNAP III, RNAP sigma70, RNAP-II, RNAP2, RNAPII, RPO, rpo1N, Rpo41, RpoA, RpoD, RpoS, RpoT, Saci_0834, sigma38 RNA polymerase, sigmaS-containing RNA polymerase, T7 RNA polymerase, T7 RNAP, T7-like RNA polymerase, Taq polymerase, transcriptase, YonO

ECTree

     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.7 Nucleotidyltransferases
                2.7.7.6 DNA-directed RNA polymerase

Crystallization

Crystallization on EC 2.7.7.6 - DNA-directed RNA polymerase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure determination
-
structure-based analysis of the evolution of archaeal and eukaryotic DNA-dependent RNA polymerases, overview
-
hanging drop vapor diffusion
crystallographic structure at 4.0 A
-
T7 RNAP elonation complex
crystal structure anaysis
-
a large fragment of subunit PA bound to a fragment of subunit PB1, hanging dropn vapour diffusion method, 20°C, mixing of 0.001 ml of protein solution, containing 10 mg/ml protein in 20 mM Tris-HCl, pH 8.0, and 100 mM sodium chloride, and 0.001 ml of reservoir solution consisting of 100 mM Tris-HCl, pH 7.5, and 2.4 M sodium formate, X-ray diffraction structure determination and analysis at 2.3 A resolution
-
hanging drop vapor diffusion
structure-based analysis of the evolution of archaeal and eukaryotic DNA-dependent RNA polymerases, overview
-
crystal structure determination
-
crystal structure determination
-
crystallization of the enzyme with DNA fragments, crystal growth is optimized using a nanoseeding technique, of the various crystals screened, one diffracts to 4.3 A resolution
-
microbatch under oil technique, hanging-drop vapour diffusion technique, crystal structure at 3.35 A resolution
vapour diffusion technique using nanolitre sitting-drop, crystal structures of the DNA-bound and free form of the enzyme
crystal structure determination, structure including the A' subunit jaw and clamp head domains and RpoG and Rpo13 subunits
-
crystal structure of the core enzyme at about 3.3 A resolution
-
free enzyme and D/L subcomplex of archaeal RNAP, X-ray diffraction structure determination and analysis at 3.4 and 1.7 A resolution, respectively
ammonium sulfate precipitation
-
crystal structure of the core enzyme at about 3.3 A resolution
-
crystallization of RNA polymerase II elongation complex. The purified paused complex forms crystals capable of X-ray diffraction to 3,5 A resolution. The complex remains active in the crystal and, in the presence of nucleoside triphosphates, can efficiently extend the transcript in situ
-
crystals are grown by the sitting drop vapor diffusion method, crystal structure of RNA polymerase II in the act of transcription is determined at 3.3 A resolution
-
glycerol precipitation, two-dimensional crystals of RNA polymerase I dimers are obtained upon interaction with positively charged lipid layers
-
hanging-drop vapour diffusion method. Complete RNA polymerase II elongation complex structure and its interactions with NTP and TFIIS
-
in complex with alpha-amanitin, hanging drop vapour diffusion method, with 200 mM ammonium acetate, 300 mM sodium acetate, 50 mM HEPES, pH 7.0, 4-7% (w/v) PEG 6000 and 5 mM Tris(2-carboxyethyl) phosphine
-
in order to obtain an atomic model of the complete Pol II, atomic models of the core Pol II at 2.8 A resolution and of the additional heterodimeric subcomplex of subunits Rpb4 and Rpb7 at 2.3 A resolution are combined and refined against the diffraction data obtained from a holo-Pol II crystal at 3.8 A resolution, method optimization
-
purified Pol II, X-ray diffraction structuredetermination and analysis at 3.8 A resolution, single anomalous diffraction from zinc ions bound intrinsically in Pol II
two-dimensional crystals are obtained by interaction with positively charged lipid layers. The enzyme is preferentially oriented by the lipid phase
-
Pol II in complex with transcription factor TFIIB, sessile drop-vapor diffusion method, 11 mg/ml protein in 10 mM Tris-HCl, pH 7.5, 25 mM KCl, 0.1 mM EDTA, 0.001 mM ZnCl2, 10 mM DTT, and 14.2 mM pentaethyleneglycol monooctyl ether, is mixed with an equal volume of reservoir solution containing 50 mM MES, pH 6.3, 300 mM ammonium acetate, 5-6.5% w/v PEG 4000, and 10 mM DTT, 9 days at 16°C, crystals are crushed and microseeded into a fresh drop prepared as before except with MES, pH 6.6, and 3.6% PEG 4000. After several rounds of microseeding, long rod-shaped crystals are obtained, cryoprotection by 15-30% glycerol, X-ray difraction structure determination and analysis at 3.65 A resolution. molecular modelling
purified recombinant DNA-directed RNA polymerase subunit L, hanging drop vapour diffusion method, mixing of 15 mg/ml protein in a buffer consisting of 25 mM Tris-HCl, pH 7.5, 15 mM NaCl, 3 mM 2-mercaptoethanol, with 500 nl reservoir solution containing 0.2 M lithium sulfate, 21% w/v PEG 3350, 15% v/v MPD, 0.1 M imidazole-HCl, pH 6.0, and equilibration against 0.07 ml of reservoir solution, 10-14°C, X-ray diffraction structure determination and analysis at 2.1 A resolution
crystal structure of the core enzyme at 3.3 A resolution
-
sitting-drop vapor diffusion technique, cocrystallization of the Thermus thermophilus RNAP holoenzyme and gp39