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| | ==Crystal structure of DmTailor in complex with CACAGU RNA== | | ==Crystal structure of DmTailor in complex with CACAGU RNA== |
| - | <StructureSection load='6i0v' size='340' side='right' caption='[[6i0v]], [[Resolution|resolution]] 1.85Å' scene=''> | + | <StructureSection load='6i0v' size='340' side='right'caption='[[6i0v]], [[Resolution|resolution]] 1.85Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6i0v]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6I0V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6I0V FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6i0v]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6I0V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6I0V FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.851Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6i0s|6i0s]], [[6i0t|6i0t]], [[6i0u|6i0u]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/RNA_uridylyltransferase RNA uridylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.52 2.7.7.52] </span></td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6i0v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6i0v OCA], [https://pdbe.org/6i0v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6i0v RCSB], [https://www.ebi.ac.uk/pdbsum/6i0v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6i0v ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6i0v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6i0v OCA], [http://pdbe.org/6i0v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6i0v RCSB], [http://www.ebi.ac.uk/pdbsum/6i0v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6i0v ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TUTT_DROME TUTT_DROME]] Uridylyltransferase which mediates terminal uridylation of miRNAs, leading to their degradation. Has high specificity for splicing-derived miRNAs (mirtrons) and other miRNA substrates containing a 3'-G terminal nucleotide. Appears to be a major suppressor of mirtron biogenesis.<ref>PMID:26145174</ref> <ref>PMID:26145176</ref> | + | [https://www.uniprot.org/uniprot/TUTT_DROME TUTT_DROME] Uridylyltransferase which mediates terminal uridylation of miRNAs, leading to their degradation. Has high specificity for splicing-derived miRNAs (mirtrons) and other miRNA substrates containing a 3'-G terminal nucleotide. Appears to be a major suppressor of mirtron biogenesis.<ref>PMID:26145174</ref> <ref>PMID:26145176</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6i0v" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6i0v" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[RNA uridylyltransferase|RNA uridylyltransferase]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: RNA uridylyltransferase]] | + | [[Category: Drosophila melanogaster]] |
| - | [[Category: Ivascu, A]] | + | [[Category: Large Structures]] |
| - | [[Category: Jinek, M]] | + | [[Category: Ivascu A]] |
| - | [[Category: Kroupova, A]]
| + | [[Category: Jinek M]] |
| - | [[Category: Nucleotidyl transferase]] | + | [[Category: Kroupova A]] |
| - | [[Category: Terminal uridyl transferase]] | + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
TUTT_DROME Uridylyltransferase which mediates terminal uridylation of miRNAs, leading to their degradation. Has high specificity for splicing-derived miRNAs (mirtrons) and other miRNA substrates containing a 3'-G terminal nucleotide. Appears to be a major suppressor of mirtron biogenesis.[1] [2]
Publication Abstract from PubMed
Non-templated 3'-uridylation of RNAs has emerged as an important mechanism for regulating the processing, stability and biological function of eukaryotic transcripts. In Drosophila, oligouridine tailing by the terminal uridylyl transferase (TUTase) Tailor of numerous RNAs induces their degradation by the exonuclease Dis3L2, which serves functional roles in RNA surveillance and mirtron RNA biogenesis. Tailor preferentially uridylates RNAs terminating in guanosine or uridine nucleotides but the structural basis underpinning its RNA substrate selectivity is unknown. Here, we report crystal structures of Tailor bound to a donor substrate analog or mono- and oligouridylated RNA products. These structures reveal specific amino acid residues involved in donor and acceptor substrate recognition, and complementary biochemical assays confirm the critical role of an active site arginine in conferring selectivity toward 3'-guanosine terminated RNAs. Notably, conservation of these active site features suggests that other eukaryotic TUTases, including mammalian TUT4 and TUT7, might exhibit similar, hitherto unknown, substrate selectivity. Together, these studies provide critical insights into the specificity of 3'-uridylation in eukaryotic post-transcriptional gene regulation.
Structural basis for acceptor RNA substrate selectivity of the 3' terminal uridylyl transferase Tailor.,Kroupova A, Ivascu A, Reimao-Pinto MM, Ameres SL, Jinek M Nucleic Acids Res. 2018 Nov 20. pii: 5193338. doi: 10.1093/nar/gky1164. PMID:30462292[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Bortolamiol-Becet D, Hu F, Jee D, Wen J, Okamura K, Lin CJ, Ameres SL, Lai EC. Selective Suppression of the Splicing-Mediated MicroRNA Pathway by the Terminal Uridyltransferase Tailor. Mol Cell. 2015 Jul 16;59(2):217-28. doi: 10.1016/j.molcel.2015.05.034. Epub 2015 , Jul 2. PMID:26145174 doi:http://dx.doi.org/10.1016/j.molcel.2015.05.034
- ↑ Reimao-Pinto MM, Ignatova V, Burkard TR, Hung JH, Manzenreither RA, Sowemimo I, Herzog VA, Reichholf B, Farina-Lopez S, Ameres SL. Uridylation of RNA Hairpins by Tailor Confines the Emergence of MicroRNAs in Drosophila. Mol Cell. 2015 Jul 16;59(2):203-16. doi: 10.1016/j.molcel.2015.05.033. Epub 2015 , Jul 2. PMID:26145176 doi:http://dx.doi.org/10.1016/j.molcel.2015.05.033
- ↑ Kroupova A, Ivascu A, Reimao-Pinto MM, Ameres SL, Jinek M. Structural basis for acceptor RNA substrate selectivity of the 3' terminal uridylyl transferase Tailor. Nucleic Acids Res. 2018 Nov 20. pii: 5193338. doi: 10.1093/nar/gky1164. PMID:30462292 doi:http://dx.doi.org/10.1093/nar/gky1164
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