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| | ==Crystal structure of Tailor== | | ==Crystal structure of Tailor== |
| - | <StructureSection load='5z4c' size='340' side='right' caption='[[5z4c]], [[Resolution|resolution]] 1.65Å' scene=''> | + | <StructureSection load='5z4c' size='340' side='right'caption='[[5z4c]], [[Resolution|resolution]] 1.65Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5z4c]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Z4C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Z4C FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5z4c]] is a 1 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=5Z4C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5Z4C FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Tailor, CG1091 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</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]] 1.65Å</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=5z4c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5z4c OCA], [https://pdbe.org/5z4c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5z4c RCSB], [https://www.ebi.ac.uk/pdbsum/5z4c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5z4c 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=5z4c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5z4c OCA], [http://pdbe.org/5z4c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5z4c RCSB], [http://www.ebi.ac.uk/pdbsum/5z4c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5z4c 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 5z4c" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5z4c" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[RNA uridylyltransferase|RNA uridylyltransferase]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Drome]] | + | [[Category: Drosophila melanogaster]] |
| - | [[Category: RNA uridylyltransferase]] | + | [[Category: Large Structures]] |
| - | [[Category: Cheng, L]] | + | [[Category: Cheng L]] |
| - | [[Category: Gong, Q]] | + | [[Category: Gong Q]] |
| - | [[Category: Jiang, Y]] | + | [[Category: Jiang Y]] |
| - | [[Category: Li, F]] | + | [[Category: Li F]] |
| - | [[Category: Shi, Y]] | + | [[Category: Shi Y]] |
| - | [[Category: Xie, C]] | + | [[Category: Xie C]] |
| - | [[Category: Yu, H]] | + | [[Category: Yu H]] |
| - | [[Category: Terminal uridylyltransferase]]
| + | |
| - | [[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
Terminal uridylyl transferase (TUTase) is one type of enzyme that modifies RNA molecules by facilitating the post-transcriptional addition of uridyl ribonucleotides to their 3' ends. Recent researches have reported that Drosophila TUTase, Tailor, exhibits an intrinsic preference for RNA substrates ending in 3'G, distinguishing it from any other known TUTases. Through this unique feature, Tailor plays a crucial role as the repressor in the biogenesis pathway of splicing-derived mirtron pre-miRNAs. Here we describe crystal structures of core catalytic domain of Tailor and its complexes with RNA stretches 5'-AGU-3' and 5'-AGUU-3'. We demonstrate that R327 and N347 are two key residues contributing cooperatively to Tailor's preference for 3'G, and R327 may play an extra role in facilitating the extension of polyuridylation chain. We also demonstrate that conformational stability of the exit of RNA-binding groove also contributes significantly to Tailor's activity. Overall, our work reveals useful insights to explain why Drosophila Tailor can preferentially select RNA substrates ending in 3'G and provides important values for further understanding the biological significances of biogenesis pathway of mirtron in flies.
Structural insights into a unique preference for 3' terminal guanine of mirtron in Drosophila TUTase tailor.,Cheng L, Li F, Jiang Y, Yu H, Xie C, Shi Y, Gong Q Nucleic Acids Res. 2018 Nov 8. pii: 5165274. doi: 10.1093/nar/gky1116. PMID:30407553[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
- ↑ Cheng L, Li F, Jiang Y, Yu H, Xie C, Shi Y, Gong Q. Structural insights into a unique preference for 3' terminal guanine of mirtron in Drosophila TUTase tailor. Nucleic Acids Res. 2018 Nov 8. pii: 5165274. doi: 10.1093/nar/gky1116. PMID:30407553 doi:http://dx.doi.org/10.1093/nar/gky1116
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