2.7.7.52: RNA uridylyltransferase
This is an abbreviated version!
For detailed information about RNA uridylyltransferase, go to the full flat file.
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curriculum
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self-care
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medicine
- 2.7.7.52
-
social
- women
-
clinician
-
services
- children
-
plan
-
physician
-
fabric
-
healthcare
-
perceived
-
professionals
-
decision
-
percept
-
demographic
-
film
-
user
-
theme
-
policy
-
psychological
-
skill
-
evidence-based
-
team
-
practitioner
-
surgeon
-
nanostructures
-
decision-making
-
emotional
-
psychosocial
-
thematic
-
tunable
-
semi-structured
- nurses
-
rehabilitation
-
caregiver
-
satisfaction
-
dope
-
doping
-
stakeholder
-
semiconductor
-
self-management
-
optoelectronic
-
self-efficacy
-
sociodemographic
-
therapist
-
photoluminescence
-
violence
-
psycinfo
-
interpersonal
-
curriculum
-
self-care
- medicine
Reaction
Synonyms
3' terminal uridylyl transferase, 3'-terminal uridylyl transferase 1, At2g45620, caffeine-induced death suppressor protein 1, Cid1, GLD2, HESO1, MEAT1, mitochondrial editosome-like complex associated TUTase 1, More, RET, RET1, RET2, RNA editing TUTase, RNA silencing protein 1, Rsp1, Tailor, TbMP57 TUTase, TbTUT3, TbTUT4, terminal RNA uridylyltransferase, terminal U transferase (TUTase), terminal uridylyl transferase, terminal uridylyltransferase, terminal uridylyltransferase Tailor, TNTase CG1091, TUT, TUT1, TUT2, TUT4, TUT7, TUTase, TUTase 1, TUTase 2, TUTase 3, TUTase 4, TUTase4, TUTase6, TUTase7, U6 snRNA-specific terminal uridylyltransferase, U6-TUTase, uridylyltransferase, terminal, URT1, UTP: RNA uridylyltransferase, UTP:RNA uridylyltransferase 1, Zcchc11, ZCCHC6
ECTree
2.7.7.52 RNA uridylyltransferaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 2.7.7.52 - RNA uridylyltransferase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + 5'(ppp)-UGAGGUAGUAGGUUGUAUAGUU-3'
diphosphate + 5'(ppp)-UGAGGUAGUAGGUUGUAUAGUUA-3'
-
i.e. triphosphorylated human let-7a-5p-3p
-
-
?
ATP + 5'-UGAGGUAGUAGGUUGUAUAGUU-3'
diphosphate + 5'-UGAGGUAGUAGGUUGUAUAGUUA-3'
-
i.e. unphosphorylated human let-7a-0P. Gld2 displays an 83fold preference of ATP over UTP
-
-
?
ATP + U6 small nuclear RNA
?
isoform TUT1 incorporates UMP more efficiently than AMP into U6 small nuclear RNA transcript ending with four uridines
-
-
?
CTP + 5'(pp)-UGAGGUAGUAGGUUGUAUAGUU-3'
diphosphate + 5'(pp)-UGAGGUAGUAGGUUGUAUAGUUC-3'
-
i.e. diphosphorylated human let-7a-5p-2p
-
-
?
UTP + 5'(p)-UGAGGUAGUAGGUUGUAUAGUU-3'
diphosphate + 5'(p)-UGAGGUAGUAGGUUGUAUAGUUU-3'
-
i.e. monophosphorylated human let-7a-5p. Gld2 displays an 83fold preference of ATP over UTP
-
-
?
UTP + miR-1003-3p-G
?
22-nt single stranded RNA oligonucleotide derived from the miR-1003 stem-loop
-
-
?
UTP + miR158an
diphosphate + miR158an+1
miR158a has the sequence 5'-Cy5-UCCCAAAUGUAGACAAAGCA-3'
-
-
?
UTP + mirtronRNAn
diphosphate + mirtronRNAn+1
the enzyme preferentially catalyzes the uridylation of mirtronRNAs ending in 3'G and 3'U
-
-
?
UTP + precursor let-7 RNAn
diphosphate + precursor let-7 RNAn+1
the interaction between the Lin28:pre-let-7 complex and the N-terminal Lin28-interacting module of TUT4 is required for prelet-7 oligo-uridylylation by the C-terminal catalytic module of TUT4/7
-
-
?
UTP + precursor let-7a-1 RNAn
diphosphate + precursor let-7a-1 RNAn+1
-
-
-
?
UTP + RNAn containing a terminal G residue
diphosphate + RNAn+1
-
substrate dsRNA
-
-
?
UTP + U6 small nuclear RNA
?
isoform TUT1 incorporates UMP more efficiently than AMP into U6 small nuclear RNA transcript ending with four uridines
-
-
?
UTP + U6 snRNAn
diphosphate + U6 snRNAn+1
the enzyme builds or repairs the 3'-oligo-uridylylated tail of U6 snRNA
-
-
?
ATP + RNAn
diphosphate + RNAn+1
-
editosomal enzyme form, no activity
-
-
?
CTP + RNAn
diphosphate + RNAn+1
-
editosomal enzyme form, no activity
-
-
?
GTP + RNAn
diphosphate + RNAn+1
-
about 50% of the activity with UTP, prefers Mn2+ as divalent cation
-
-
?
GTP + RNAn
diphosphate + RNAn+1
-
editosomal enzyme form, no activity
-
-
?
UTP + miRNAn
diphosphate + miRNAn+1
the enzyme URT1 plays a redundant but important role in miRNA uridylation when HESO1 is absent
-
-
?
UTP + mRNAn
diphosphate + mRNAn+1
for mRNA, URT1 is the main enzyme to uridylate the majority of mRNA and repairs their deadenylated ends to restore the binding site for poly(A) binding protein. Enzyme HESO1, on the other hand, targets mostly the mRNAs with very short oligo(A) tails and fails in fulfilling the same task
-
-
?
UTP + mRNAn
diphosphate + mRNAn+1
for mRNA, URT1 is the main enzyme to uridylate the majority of mRNA (70-80%) and repairs their deadenylated ends to restore the binding site for poly(A) binding protein. Enzyme HESO1, on the other hand, targets mostly the mRNAs with very short oligo(A) tails and fails in fulfilling the same task
-
-
?
UTP + poly(A) tail mimic RNAn
diphosphate + poly(A) tail mimic RNAn+1
-
-
-
-
?
UTP + poly(A) tail mimic RNAn
diphosphate + poly(A) tail mimic RNAn+1
Schizosaccharomyces pombe BG 0000H6
-
-
-
-
?
UTP + RNAn
diphosphate + RNAn+1
-
small guide RNA, i.e. gRNA
-
?
UTP + RNAn
diphosphate + RNAn+1
-
marked specificity for UTP
-
?
UTP + RNAn
diphosphate + RNAn+1
-
responsible for post-transcriptional RNA editing process of mitochondrial transcripts in kinetoplastid protozoans
-
?
UTP + RNAn
diphosphate + RNAn+1
-
addition of non-coded poly(U) tail to gRNAs
-
?
UTP + RNAn
diphosphate + RNAn+1
-
enzyme preferentially uridylates mirtron hairpins
-
?
UTP + RNAn
diphosphate + RNAn+1
the enzyme exhibits an intrinsic preference for RNA substrates ending in 3'G
-
-
?
UTP + RNAn
diphosphate + RNAn+1
-
specifically modifies the 3'-UMP terminal of mammalian U6 small nuclear RNA, i.e. snRNA, structural requirements and specificity, overview
-
?
UTP + RNAn
diphosphate + RNAn+1
-
acts as a host factor to initiate RNA synthesis by poliovirus RNA polymerase in vitro
-
?
UTP + RNAn
diphosphate + RNAn+1
the enzyme mediates template-independent uridylylation at the 3'-end of RNAs
-
-
?
UTP + RNAn
diphosphate + RNAn+1
-
RNA substrate specificity, overview
-
?
UTP + RNAn
diphosphate + RNAn+1
-
editosomal enzyme form shows preference for a 3' terminal A or G, while the mitochondrial enzyme form does not
-
?
UTP + RNAn
diphosphate + RNAn+1
-
mitochondrial enzyme form adds Us at the 3' and the 5' end of the RNA
-
?
UTP + RNAn
diphosphate + RNAn+1
-
the mitochondrial enzyme adds a single U to the 3'-end of single-stranded RNA
-
?
UTP + RNAn
diphosphate + RNAn+1
-
involved in uridine insertion in the editing process of RNA
-
?
UTP + RNAn
diphosphate + RNAn+1
-
responsible for post-transcriptional RNA editing process of mitochondrial transcripts in kinetoplastid protozoans
-
?
UTP + RNAn
diphosphate + RNAn+1
-
addition of non-coded poly(U) tail to gRNAs
-
?
UTP + RNAn
diphosphate + RNAn+1
-
addition of non-coded poly(U) tail to gRNAs
-
?
UTP + RNAn
diphosphate + RNAn+1
-
addition of primarily single U to single-stranded RNA, addition of the number of Us specified by a guide RNA to insertion editing-like substrates
-
?
UTP + RNAn
diphosphate + RNAn+1
-
TbMP57 TUTase, an enzyme thought to act exclusively in U-insertion, can also function within the U-deletion cycle, after cleavage and 3'-U-exo but before U-deletional cycle
-
-
?
UTP + RNAn
diphosphate + RNAn+1
a template-independent RNA nucleotidyltransferases that specifically recognize UTP, it possesses conserved catalytic and UTP recognition domains. A single nucleoside triphosphate is bound in the active site by a complex network of interactions between amino acid residues, a magnesium ion and highly ordered water molecules with the UTPs base, ribose and phosphate moieties, structure-function analysis, overview
-
-
?
UTP + RNAn
diphosphate + RNAn+1
-
invariant arginine residues 144 and 435 positioned in the vicinity of the UTP-binding site are critical for isoform RET2 activity on single-stranded and double-stranded RNAs, as well as function in vivo. Recognition of a double-stranded RNA, which resembles a guide RNA/mRNA duplex, is further facilitated by multipoint contacts across the RET2-specific middle domain
-
-
?
UTP + RNAn
diphosphate + RNAn+1
-
TbMP57 TUTase, an enzyme thought to act exclusively in U-insertion, can also function within the U-deletion cycle, after cleavage and 3'-U-exo but before U-deletional cycle
-
-
?
UTP + RNAn
diphosphate + RNAn+1
-
the enzyme requires a single-stranded oligoribonucleotide or polyribonucleotide with a free terminal 3'-OH as primer, e.g. oligoA20, tRNAAsp, E. coli RNA, alfalafa mosaic virus RNA 4
-
?
UTP + RNAn
diphosphate + RNAn+1
-
RNA substrate specificity, overview
-
?
UTP + RNAn
diphosphate + RNAn+1
-
RNA uridylyltransferase might function in uridylating specific proteins, RNA is not a natural substrate
-
?
UTP + RNAn containing a terminal U residue
diphosphate + RNAn+1
-
substrate dsRNA
-
-
?
additional information
?
-
enzyme shows strong preference for uridine and a distributive activity for the first added nucleotides. URT1 uridylates oligoadenylated mRNAs
-
-
?
additional information
?
-
HESO1 exhibits nucleotidyl transferase activity on methylated miRNA in vitro. HESO1 has a clear preference for miR158A-U. miR158A-G is the second most preferred substrate
-
-
?
additional information
?
-
HESO1 exhibits nucleotidyl transferase activity on methylated miRNA in vitro. HESO1 has a clear preference for miR158A-U. miR158A-G is the second most preferred substrate
-
-
?
additional information
?
-
URT1 exhibits nucleotidyl transferase activity on unmethylated miRNA in vitro. URT1 shows a strong preference for miR158 ending in A, miR158A-C, miR158A-G, and miR158A-U are similarly used by URT1
-
-
?
additional information
?
-
URT1 exhibits nucleotidyl transferase activity on unmethylated miRNA in vitro. URT1 shows a strong preference for miR158 ending in A, miR158A-C, miR158A-G, and miR158A-U are similarly used by URT1
-
-
?
additional information
?
-
enzyme shows strong preference for uridine and a distributive activity for the first added nucleotides. URT1 uridylates oligoadenylated mRNAs
-
-
?
additional information
?
-
the enzyme exhibits significantly higher tailing efficiency for substrates with a 3'-terminal G or U
-
-
-
additional information
?
-
-
human Gld2 is a bona fide adenylyltransferase with only weak activity toward other nucleotides. Gld2 is a promiscuous enzyme, with activity toward miRNA, pre-miRNA, and polyadenylated RNA substrates. Gld2 shows a clear preference for ATP in the presence of all four NTPs. Apo-Gld2 activity is restricted to adding single nucleotides and processivity likely relies on additional RNA-binding proteins
-
-
?
additional information
?
-
-
enzyme interacts with a minor fraction of total RNA ligase
-
-
?
additional information
?
-
-
post-transcriptional uridylylation of guide RNAs by RNA editing TUTase 1 or RET1, a multi-functional RNA processing enzyme, and U-insertion mRNA editing by RNA editing TUTase 2 or RET2, biological functions of TUT isozymes, RNA processing in mitochondria of trypanosomes, detailed overview
-
-
?
additional information
?
-
-
UTP recognition mechanism, overview. The NTD-CTD bi-domain catalytic modules shared by TUTases and non-canonical poly(A) polymerases, ncPAPs, are quite promiscuous in NTP binding, NTP selectivity of TUTase-like catalytic modules, RNA specificity, overview
-
-
?
additional information
?
-
-
reduction of isozyme RET1 leads to decrease in edited RNA and inhibited growth, lowers the uridine insertion and leads predominantly to shorter gRNAs
-
-
?
additional information
?
-
-
down-regulation of isozyme RET2 inhibits growth and in vivo uridine insertion, but has no effect on the length of gRNAs
-
-
?
additional information
?
-
-
many editing changes are developmentally regulated
-
-
?
additional information
?
-
-
down-regulation of RET1, but not of RET2, affects length distribution of gRNA 3' oligo(U) tails
-
-
?
additional information
?
-
-
Inhibition of RNA editing by down-regulation of expression of the mitochondrial RNA editing TUTase 1 by RNA interference has profound effects on kinetoplast biogenesis in Trypanosoma brucei procyclic cells. De novo synthesis of the apocytochrome b and cytochrome oxidase subunit I proteins is no longer detectable after 3 days of RNAi. The effect on protein synthesis correlates with a decline in the levels of the assembled mitochondrial respiratory complexes III and IV, and also with cyanide-sensitive oxygen uptake. The steady-state levels of nuclear-encoded subunits of complexes III and IV are also significantly decreased. Because the levels of the corresponding mRNAs are not affected, the observed effect is likely due to an increased turnover of these imported mitochondrial proteins. This induced protein degradation is selective for components of complexes III and IV, because little effect is observed on components of the F1-F0 -ATPase complex and on several other mitochondrial proteins
-
-
?
additional information
?
-
-
post-transcriptional uridylylation of guide RNAs by RNA editing TUTase 1 or RET1, a multi-functional RNA processing enzyme, and U-insertion mRNA editing by RNA editing TUTase 2 or RET2, biological functions of TUT isozymes, RNA processing in mitochondria of trypanosomes, detailed overview
-
-
?
additional information
?
-
TUT4 substrate specificity toward nucleoside triphosphate substrates with a synthetic 5'-radiolabeled 24-mer RNA as a primer, in presence of Mg2+ ions TUT4 preferentially incorporates uridylyl residues but the reaction with CTP is also detectable, TbTUT4 incorporates only one deoxynucleotide into RNA, overview. UTP binding site structure and structure-activity analysis
-
-
?
additional information
?
-
-
UTP recognition mechanism, overview. UTP specificity is determined primarily by the two closely positioned carboxylic residues, D297/D421 and E300/E424, which coordinate a crucial water molecule indicated in TUT4/RET2, uracil base interactions with invariant amino acids N147, S148, Y189, D297, E300 of TUT4. The NTD-CTD bi-domain catalytic modules shared by TUTases and non-canonical poly(A) polymerases, ncPAPs, are quite promiscuous in NTP binding, NTP selectivity of TUTase-like catalytic modules, RNA specificity, overview
-
-
?
additional information
?
-
-
isoform RET1 adds U tails to gRNAs, rRNAs, and selected mRNAs and contributes U residues into A/U heteropolymers. Isoform RET1's terminal uridylyl transferase activity is required for the nucleolytic processing of gRNA, rRNA, and mRNA precursors. The U tails presence does not affect the stability of gRNAs and rRNAs, while transcript-specific uridylylation triggers 3' to 5' mRNA decay. The minicircle-encoded antisense transcripts, which are stabilized by RET1-catalyzed uridylylation, may direct a nucleolytic cleavage of multicistronic precursors
-
-
?
additional information
?
-
-
recombinant RET2 catalyzes a faithful editing on gapped precleaved double-stranded RNA substrates, and this reaction requires an internal monophosphate group at the 5' end of the mRNA 3' cleavage fragment. RET2 processivity is limited to insertion of three U residues. Incorporation into the RNA editing core complex RECC allows filling of longer gaps similar to those observed in vivo. Monomeric and RECC-embedded enzymes display a similar bimodal activity, the distributive insertion of a single uracil is followed by a processive extension limited by the number of guiding nucleotides. The distributive +1 insertion creates a substrate for the processive gap-filling reaction. Upon base-pairing of the +1 extended 5' cleavage fragment with a guiding nucleotide, this substrate is recognized by RET2 in a different mode compared to the product of the initial nucleolytic cleavage. Therefore, RET2 distinguishes base pairs in gapped RNA substrates
-
-
?
