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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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