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AMUTP + 5'-FAM-labeled RNA
?
-
-
-
-
?
APUTP + 5'-FAM-labeled RNA
?
-
-
-
-
?
ATP + (mRNA)n
diphosphate + (mRNA)n+1
-
i.e. total human mRNA
-
-
?
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 + RNAn
diphosphate + RNAn+1
ATP + U6 small nuclear RNA
?
isoform TUT1 incorporates UMP more efficiently than AMP into U6 small nuclear RNA transcript ending with four uridines
-
-
?
ATUTP + 5'-FAM-labeled RNA
?
-
-
-
-
?
CTP + 5'(pp)-UGAGGUAGUAGGUUGUAUAGUU-3'
diphosphate + 5'(pp)-UGAGGUAGUAGGUUGUAUAGUUC-3'
-
i.e. diphosphorylated human let-7a-5p-2p
-
-
?
CTP + RNAn
diphosphate + RNAn+1
GTP + miR-122
diphosphate + ?
-
-
-
-
?
GTP + RNAn
diphosphate + RNAn+1
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 + 5'-Cy5-GUGGGUAUCUGGGAGAUUACAUAUUCACAG-3'
?
-
-
-
?
UTP + 5'-FAM-labeled RNA
?
-
-
-
-
?
UTP + 5-Cy5-CAUAUUCACAG-3'
?
-
-
-
?
UTP + miR-1003 RNAn
diphosphate + miR-1003 RNAn+1
-
-
-
?
UTP + miR-1003-3p-G
?
22-nt single stranded RNA oligonucleotide derived from the miR-1003 stem-loop
-
-
?
UTP + miR-324n
diphosphate + miR-324n+1
-
-
-
?
UTP + miR158an
diphosphate + miR158an+1
miR158a has the sequence 5'-Cy5-UCCCAAAUGUAGACAAAGCA-3'
-
-
?
UTP + miRNAn
diphosphate + miRNAn+1
UTP + mirtronRNAn
diphosphate + mirtronRNAn+1
the enzyme preferentially catalyzes the uridylation of mirtronRNAs ending in 3'G and 3'U
-
-
?
UTP + mRNAn
diphosphate + mRNAn+1
UTP + poly(A) tail mimic RNAn
diphosphate + poly(A) tail mimic RNAn+1
UTP + pre-miRNAn
diphosphate + pre-miRNAn+1
UTP + precursor let-7 RNA
?
-
-
-
?
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
diphosphate + RNAn+1
UTP + RNAn containing a terminal G residue
diphosphate + RNAn+1
-
substrate dsRNA
-
-
?
UTP + RNAn containing a terminal U residue
diphosphate + RNAn+1
UTP + sgRNAn
diphosphate + sgRNAn+1
-
-
-
-
?
UTP + tRNAn
diphosphate + tRNAn+1
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
-
-
?
additional information
?
-
ATP + RNAn
diphosphate + RNAn+1
-
low activity
-
-
?
ATP + RNAn
diphosphate + RNAn+1
-
editosomal enzyme form, no activity
-
-
?
CTP + RNAn
diphosphate + RNAn+1
-
-
-
-
?
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
-
-
-
-
?
UTP + miRNAn
diphosphate + miRNAn+1
the enzyme URT1 plays a redundant but important role in miRNA uridylation when HESO1 is absent
-
-
?
UTP + miRNAn
diphosphate + miRNAn+1
-
-
-
-
?
UTP + miRNAn
diphosphate + miRNAn+1
-
-
-
?
UTP + miRNAn
diphosphate + miRNAn+1
-
-
-
-
?
UTP + miRNAn
diphosphate + miRNAn+1
-
-
-
-
?
UTP + miRNAn
diphosphate + miRNAn+1
-
-
-
-
?
UTP + miRNAn
diphosphate + miRNAn+1
-
-
-
-
?
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 + mRNAn
diphosphate + mRNAn+1
-
-
-
-
?
UTP + mRNAn
diphosphate + mRNAn+1
-
-
-
-
?
UTP + mRNAn
diphosphate + mRNAn+1
-
-
-
-
?
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
-
-
-
-
?
UTP + pre-miRNAn
diphosphate + pre-miRNAn+1
-
-
-
-
?
UTP + pre-miRNAn
diphosphate + pre-miRNAn+1
-
-
-
-
?
UTP + RNAn
diphosphate + RNAn+1
-
-
-
?
UTP + RNAn
diphosphate + RNAn+1
-
-
-
?
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
-
-
-
?
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
-
3'-poly(A) of virion RNA
-
?
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
-
-
-
?
UTP + RNAn
diphosphate + RNAn+1
-
-
-
-
?
UTP + RNAn
diphosphate + RNAn+1
-
RNA substrate specificity, overview
-
?
UTP + RNAn
diphosphate + RNAn+1
-
-
-
?
UTP + RNAn
diphosphate + RNAn+1
-
-
-
?
UTP + RNAn
diphosphate + RNAn+1
-
-
-
-
?
UTP + RNAn
diphosphate + RNAn+1
-
-
-
?
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
-
kinetoplast 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
-
marked specificity for UTP
-
?
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
-
-
-
-
?
UTP + RNAn containing a terminal U residue
diphosphate + RNAn+1
-
substrate dsRNA
-
-
?
UTP + tRNAn
diphosphate + tRNAn+1
-
-
-
-
?
UTP + tRNAn
diphosphate + tRNAn+1
-
-
-
-
?
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
?
-
the enzyme has no activity with ATP
-
-
-
additional information
?
-
-
the enzyme has no activity with ATP
-
-
-
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
?
-
-
-
-
-
?
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
UTP + miR-1003 RNAn
diphosphate + miR-1003 RNAn+1
-
-
-
?
UTP + miR-324n
diphosphate + miR-324n+1
-
-
-
?
UTP + miRNAn
diphosphate + miRNAn+1
UTP + mRNAn
diphosphate + mRNAn+1
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 + RNAn
diphosphate + RNAn+1
UTP + sgRNAn
diphosphate + sgRNAn+1
-
-
-
-
?
UTP + U6 snRNAn
diphosphate + U6 snRNAn+1
the enzyme builds or repairs the 3'-oligo-uridylylated tail of U6 snRNA
-
-
?
additional information
?
-
UTP + miRNAn
diphosphate + miRNAn+1
-
-
-
-
?
UTP + miRNAn
diphosphate + miRNAn+1
-
-
-
-
?
UTP + miRNAn
diphosphate + miRNAn+1
-
-
-
?
UTP + miRNAn
diphosphate + miRNAn+1
-
-
-
-
?
UTP + miRNAn
diphosphate + miRNAn+1
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
?
UTP + RNAn
diphosphate + RNAn+1
the enzyme exhibits an intrinsic preference for RNA substrates ending in 3'G
-
-
?
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
-
-
-
?
UTP + RNAn
diphosphate + RNAn+1
-
-
-
?
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
-
RNA uridylyltransferase might function in uridylating specific proteins, RNA is not a natural substrate
-
?
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
?
-
-
-
-
-
?
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
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additional information
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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
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malfunction
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enzyme deletion increases sensitivity to protein misfolding stress
malfunction
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enzyme deletion increases sensitivity to protein misfolding stress
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metabolism
isoform TUT1 catalyzes oligo-uridylylation of U6 small nuclear RNA, which catalyzes mRNA splicing. Oligo-uridylylation of U6 snRNA is required for U6 snRNA maturation, U4/U6-di-snRNP formation, and U6 snRNA recycling during mRNA splicing
metabolism
isoform TUT4 catalyzes mono- or oligo-uridylylation of precursor let-7 (pre-let-7). Let-7 RNA is broadly expressed in somatic cells and regulates cellular proliferation and differentiation. Mono-uridylylation of pre-let-7 by TUT4 promotes subsequent Dicer processing to up-regulate let-7 biogenesis
metabolism
isoform TUT7 catalyzes mono- or oligo-uridylylation of precursor let-7 (pre-let-7). Let-7 RNA is broadly expressed in somatic cells and regulates cellular proliferation and differentiation. Mono-uridylylation of pre-let-7 by TUT7 promotes subsequent Dicer processing to up-regulate let-7 biogenesis
metabolism
the enzyme plays a crucial role as the repressor in the biogenesis pathway of splicing-derived mirtron pre-miRNAs
metabolism
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the enzyme uridylates polyadenylated mRNAs to trigger Lsm1-7-mediated decapping of the RNA 5'-end and subsequent degradation by the U-specific exonuclease Dis3L2
metabolism
the U6 snRNA-specific terminal uridylyltransferase is required for pre-mRNA splicing
metabolism
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the enzyme uridylates polyadenylated mRNAs to trigger Lsm1-7-mediated decapping of the RNA 5'-end and subsequent degradation by the U-specific exonuclease Dis3L2
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physiological function
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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
physiological function
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isoform RET2 is an integral component of the RNA editing core complex RECC. Interaction of RET2 with RECC is accomplished via a protein-protein contact between its middle domain and structural subunit MP81. The 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 RECC voids the internal phosphate requirement and 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
physiological function
isoform Rsp1 associates with uridylyltransferase Rdn1-RNA-dependent RNA polymerase Rdf1 or Rdn1-Rdf2 subcomplexes, creating Rsp1 complexes RSPCs that are physically separate from RNA-dependent RNA polymerase complexes RDRCs. The uridylyltransferase activity of Rdn1 is greatly reduced in RSPCs compared with RDRCs, suggesting enzyme regulation by the alternative partners. Despite the loss of all known RDRC-generated classes of endogenous sRNAs, RSP1 gene knockout is tolerated in growing cells. A minority class of dicer protein Dcr2-dependent sRNAs persists in cells lacking Rsp1 with increased size heterogeneity
physiological function
isoforms TUT7/ZCCHC6, TUT4/ZCCHC11, and TUT2/PAPD4/GLD2 are the terminal uridylyltransferases responsible for pre-miRNA mono-uridylation. The terminal uridylyl transferases act specifically on dsRNAs with a 1 nucleotide 3' overhang, thereby creating a 2 nucleotide 3' overhang. Depletion of terminal uridylyl transferases reduces let-7 microRNA levels and disrupts let-7 function. Although the let-7 suppressor, Lin28, induces inhibitory oligo-uridylation in embryonic stem cells, mono-uridylation occurs in somatic cells lacking Lin28 to promote let-7 biogenesis
physiological function
isoforms Zcchc11 and Zcchc6 redundantly control let-7 biogenesis in embryonic stem cells
physiological function
isoform HESO1, which uridylates most unmethylated miRNAs in vivo, and isoform URT1 which exhibits nucleotidyl transferase activity on unmethylated miRNA, prefer substrates with different 3'-end nucleotides in vitro and act cooperatively to tail different forms of the same miRNAs in vivo. Both HESO1 and URT1 exhibit nucleotidyl transferase activity on AGO1-bound miRNAs. Although the enzymes are able to add long tails to AGO1-bound miRNAs, the tailed miRNAs remain associated with AGO1. Tailing of AGO1-bound miRNA165/6 drastically reduces the slicing activity of AGO1-miR165/6
physiological function
isoform Tailor preferentially uridylates mirtron hairpins, thereby impeding the production of non-canonical microRNAs. Mirtron selectivity is explained by primary sequence specificity of Tailor, selecting substrates ending with a 3'-guanosine. In contrast to mirtrons, conserved Drosophila precursor micro-RNAs are significantly depleted in 3'-guanosine, thereby escaping regulatory uridylation. Cytoplasmic Tailor is required for miRNA uridylation and normal fertility in flies
physiological function
oligo(A)-tailed mRNAs are uridylated by the cytosolic UTP:RNA uridylyltransferase URT1, and URT1 has no major impact on mRNA degradation rates. In absence of uridylation, oligo(A) tails are trimmed, indicating that uridylation protects oligoadenylated mRNAs from 3'-ribonucleolytic attacks. URT1 mutants display an increase in 3'-truncated transcripts
physiological function
URT1 is the single most predominant nucleotidyl transferase that tails miRNAs. URT1 and isoform HESO1, which uridylates most unmethylated miRNAs in vivo, prefer substrates with different 3'-end nucleotides in vitro and act cooperatively to tail different forms of the same miRNAs in vivo. Both HESO1 and URT1 exhibit nucleotidyl transferase activity on AGO1-bound miRNAs. Although the enzymes are able to add long tails to AGO1-bound miRNAs, the tailed miRNAs remain associated with AGO1. Tailing of AGO1-bound miRNA165/6 drastically reduces the slicing activity of AGO1-miR165/6. Monouridylation of miR171a by URT1 endows the miRNA the ability to trigger the biogenesis of secondary siRNAs
physiological function
isoform TUT4 uridylates pre-miR-324, resulting in alternative processing by DICER. The altered cleavage leads to selection of the 3p strand instead of the 5p strand. Perturbation of the miR-324 arm usage disrupts glioblastoma cell proliferation
physiological function
isoform TUT7 uridylates pre-miR-324, resulting in alternative processing by DICER. The altered cleavage leads to selection of the 3p strand instead of the 5p strand. Perturbation of the miR-324 arm usage disrupts glioblastoma cell proliferation
physiological function
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oligo(A)-tailed mRNAs are uridylated by the cytosolic UTP:RNA uridylyltransferase URT1, and URT1 has no major impact on mRNA degradation rates. In absence of uridylation, oligo(A) tails are trimmed, indicating that uridylation protects oligoadenylated mRNAs from 3'-ribonucleolytic attacks. URT1 mutants display an increase in 3'-truncated transcripts
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mutant enzyme D547A, sitting drop vapor diffusion method, using 0.1 M HEPES, pH 7.5, 10% (w/v) PEG 6000 and 5% (w/v) 2-methyl-2,4-pentanediol
enzyme bound to uridine-5'-[(alpha,beta)-imido]triphosphate, hanging drop vapor diffusion method, using 20% (v/v) glycerol ethoxylate. Enzyme bound to GpU, sitting drop vapor diffusion method, using 30% (v/v) glycerol ethoxylate and 60 mM sodium malonate, pH 7.0. Enzyme bound to CACAGU, hanging drop vapor diffusion method, using 35% (v/v) glycerol ethoxylate and 75 mM sodium malonate, pH 7.0. Enzyme bound to U6 RNA, sitting drop vapor diffusion method, using 35% (v/v) glycerol ethoxylate and 90 mM sodium malonate, pH 7.0
enzyme residues 202-560 and enzyme in complex with RNA stretches 5 -AGU-3 and 5 -AGUU-3 , sitting drop vapor diffusion method, using 0.1 M Tris-HCl, pH 8.4, 50 mM NaCl, 0.2 M lithium sulfate monohydrate and 15% (w/v) PEG3350
apoenzyme and enzyme in complex with UTP or ATP, hanging drop vapor diffusion method, using 13-15% (w/v) PEG3350 as the precipitant
Lin28-interacting module of TUT4, sitting drop vapor diffusion method, using 100 mM HEPES-NaOH, pH 7.0, 20% (w/v) PEG3350, 3% (v/v) 2-methyl-2,4-pentanediol, 200mM ammonium citrate, and 3% (w/v) 1,5 diaminopentane dihydrochloride
purified recombinant N-terminally His-tagged TUT4, free or with bound 2'-deoxyribonucleoside, at a concentration of 10 mg/mL in 10 mM HEPES, pH 7.6, 70 mM KCl, 0.5 mM DTT, and in presence of 4 mM MgCl2 and 0.05 mM UTP, screening with commercial crystallization screens, vapor diffusion technique, 4°C, cryoprotection by 15% glycerol, X-ray diffraction structure determination and analysis at 2.0-2.4 A resolution
small plate-like co-crystals of purified recombinant N-terminally His-tagged TbTUT4 and UTP grow in 100 mM sodium cacodylate (pH 6.5), 200 mM calcium acetate, 18% (w/v) PEG-8000, crystal structure reveals two significantly different conformations of this TUTase:one molecule is in a relatively open apo confirmation, whereas the other displays a more compact TUTase-UTP complex
structure of apoenzyme and in complex with UTP, to 1.56 A and 1.95 A resolution, respectively. Enzyme possesses a bridging domain, which extends from the C-terminal domain and makes hydrophobic contacts with the N-terminal domain, thereby creating a cavity adjacent to the UTP-binding site. Enzyme shows no appreciable conformational change upon UTP binding and apparently does not require RNA substrate to select a cognate nucleoside triphosphate.
TUT4 in complex with UTP, X-ray diffraction structure analysis
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D491A/D493A
complete loss of activity
D547A
catalytically dead mutant
D491A/D493A
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complete loss of activity
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D280A
the mutation abrogates enzyme activity
H294A
the enzymatic activity of the mutant is reduced by about 61% as compared to the wild type enzyme
N347A
the uridylation efficiency of the mutant is reduced dramatically to about 7% when compared with that of wild type enzyme
Q519A
the activity of the mutant is reduced compared to the wild type enzyme. The mutant tails 3'-G, 3'-A and 3'-C substrates with comparable efficiencies
R295A
the enzymatic activity of the mutant is reduced by about 84% as compared to the wild type enzyme
R295K
the enzymatic activity of the mutant is reduced by about 80% as compared to the wild type enzyme
V328I
the mutation barely affects the enzyme's binding with RNA substrate and also exhibits a obvious reduction in uridylation efficiency as compared to the wild type enzyme
V328L
the mutation entirely abolishes the enzyme's catalytic activity for truncated miR-1003 bearing 3'G. The mutation barely affects the enzyme's binding with RNA substrate
V328R
the mutation entirely abolishes the enzyme's catalytic activity for truncated miR-1003 bearing 3'G. The mutation barely affects the enzyme's binding with RNA substrate
C306A/C309A
the mutant does not oligo-uridylylate pre-let-7a-1 RNA in the presence of Lin28A
H405A/K452A
the mutant shows reduced oligo-uridylylation of pre-let-7a-1 RNA in the presence of Lin28A compared to the wild type enzyme
K321A/K324A
the mutant shows severely reduced oligo-uridylylation of pre-let-7a-1 RNA in the presence of Lin28A compared to the wild type enzyme
K326A/R327A
the mutant shows severely reduced oligo-uridylylation of pre-let-7a-1 RNA in the presence of Lin28A compared to the wild type enzyme
K329A/K330A
the mutant shows strongly reduced oligo-uridylylation of pre-let-7a-1 RNA in the presence of Lin28A compared to the wild type enzyme
R669A/R670A
the mutant shows strongly reduced oligo-uridylylation of pre-let-7a-1 RNA in the presence of Lin28A compared to the wild type enzyme
R779A/R783A
the mutations reduce the RNA-binding and uridylylation activities of the enzyme
R871A/K874A
the mutations reduce the RNA-binding activity of the enzyme
C83F
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230% of wild-type activity for transfer to terminal U residue
D297A
Km=0.1728 (UTP), kcat=0.00033/sec (UTP)
D297N
Km=0.0139 (UTP), kcat=0.0000666/sec (UTP)
D97A
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complete inactivation of uridylyl transfer
E300A
Km=0.3084 (UTP), kcat=0.0066/sec (UTP)
K149A
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mutant retains partial activity
N147A
Km=0.1153 (UTP), kcat=0.005/sec (UTP)
R121A
Km=0.0028 (UTP), kcat=0.000033/sec (UTP),Km=0.132 (RNA), kcat= 0.005/sec (RNA)
R144A
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almost complete inactivation of uridylyl transfer
R307A
Km=0.0004 (UTP), kcat=0.000133/sec (UTP), Km=0.01 (RNA), kcat= 0.00833/sec (RNA)
R435A
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almost complete inactivation of uridylyl transfer
S148A
Km=0.0873 (UTP), kcat=0.021/sec (UTP), Km=0.0002 (RNA), kcat= 0.0166/sec (RNA)
S188A
Km=0.034 (UTP), kcat=0.0005/sec (UTP), Km=0.0003 (RNA), kcat= 0.00166/sec (RNA)
V271R
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10-20% of wild-type activity
V271R/C83F
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240% of wild-type activity for transfer to terminal U residue
Y189F
Km=0.0213 (UTP), kcat=0.015/sec (UTP)
Y319A
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complete inactivation of uridylyl transfer
additional information
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mutations of metal coordinating catalytic aspartic residues D66, D68 and D136, render TUT4 inactive but have no effect on UTP binding
R327A
the activity of the mutant is reduced compared to the wild type enzyme. The mutant shows clear abrogation of the 3'-G specificity, whereby the 3'-G substrate is uridylated less readily than the 3'-U, 3'-A and 3'-C substrates
R327A
the uridylation efficiency of the mutant is reduced dramatically to about 4% when compared with that of wild type enzyme
R327K
the activity of the mutant is reduced compared to the wild type enzyme but the mutant shows selectivity for 3'-G and 3'-U RNA substrates, similar to the wild type enzyme
R327K
the uridylation efficiency of the mutant is reduced dramatically to about 4% when compared with that of wild type enzyme
R141A
Km=0.001 (UTP), kcat=0.00011/sec (UTP),Km=0.0726 (RNA), kcat= 0.0216/sec (RNA)
R141A
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almost complete inactivation of uridylyl transfer
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The Leishmania kinetoplast-mitochondrion contains terminal uridylyltransferase and RNA ligase activities
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Crithidia fasciculata
-
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Trypanosome mitochondrial 3' terminal uridylyl transferase (TUTase): the key enzyme in U-insertion/deletion RNA editing
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brenda
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TbMP57 is a 3' terminal uridylyl transferase (TUTase) of the Trypanosoma brucei editosome
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2003
Trypanosoma brucei
brenda
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Biochemical characterization of a U6 small nuclear RNA-specific terminal uridylyltransferase
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270
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2003
Homo sapiens
brenda
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A tale of two TUTases
Proc. Natl. Acad. Sci. USA
100
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2003
Trypanosoma brucei
brenda
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Two distinct roles for terminal uridylyl transferases in RNA editing
Proc. Natl. Acad. Sci. USA
100
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2003
Trypanosoma brucei
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Multiple terminal uridylyltransferases of trypanosomes
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