8q66: Difference between revisions
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The | ==Crystal Structure of the C. elegans MUT-7 MUT-8 CTD complex== | ||
<StructureSection load='8q66' size='340' side='right'caption='[[8q66]], [[Resolution|resolution]] 2.03Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8q66]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8Q66 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8Q66 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.03Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=8q66 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8q66 OCA], [https://pdbe.org/8q66 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8q66 RCSB], [https://www.ebi.ac.uk/pdbsum/8q66 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8q66 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/MUT7_CAEEL MUT7_CAEEL] Represses the transposition of Tc1, Tc3, Tc4, and Tc5, perhaps by degrading transposon-specific messages. Also affects sperm development, sensitivity to RNAi of mainly germline expressed genes, silencing of some germline transgenes, X chromosome loss, and is required for cosuppression (functional silencing of chromosomal loci induced by transgenes) and for silencing induced by antisense RNA oligomers.<ref>PMID:10535732</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The MUT-7 family of 3'-5' exoribonucleases is evolutionarily conserved across the animal kingdom and plays essential roles in small RNA production in the germline. Most MUT-7 homologues carry a C-terminal domain of unknown function named MUT7-C appended to the exoribonuclease domain. Our analysis shows that the MUT7-C is evolutionary ancient, as a minimal version of the domain exists as an individual protein in prokaryotes. In animals, MUT7-C has acquired an insertion that diverged during evolution, expanding its functions. Caenorhabditis elegans MUT-7 contains a specific insertion within MUT7-C, which allows binding to MUT-8 and, consequently, MUT-7 recruitment to germ granules. In addition, in C. elegans and human MUT-7, the MUT7-C domain contributes to RNA binding and is thereby crucial for ribonuclease activity. This RNA-binding function most likely represents the ancestral function of the MUT7-C domain. Overall, this study sheds light on MUT7-C and assigns two functions to this previously uncharacterized domain. | |||
MUT-7 exoribonuclease activity and localization are mediated by an ancient domain.,Busetto V, Pshanichnaya L, Lichtenberger R, Hann S, Ketting RF, Falk S Nucleic Acids Res. 2024 Aug 27;52(15):9076-9091. doi: 10.1093/nar/gkae610. PMID:39188014<ref>PMID:39188014</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 8q66" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Caenorhabditis elegans]] | |||
[[Category: Large Structures]] | |||
[[Category: Busetto V]] | |||
[[Category: Falk S]] | |||
Latest revision as of 08:03, 18 September 2024
Crystal Structure of the C. elegans MUT-7 MUT-8 CTD complexCrystal Structure of the C. elegans MUT-7 MUT-8 CTD complex
Structural highlights
FunctionMUT7_CAEEL Represses the transposition of Tc1, Tc3, Tc4, and Tc5, perhaps by degrading transposon-specific messages. Also affects sperm development, sensitivity to RNAi of mainly germline expressed genes, silencing of some germline transgenes, X chromosome loss, and is required for cosuppression (functional silencing of chromosomal loci induced by transgenes) and for silencing induced by antisense RNA oligomers.[1] Publication Abstract from PubMedThe MUT-7 family of 3'-5' exoribonucleases is evolutionarily conserved across the animal kingdom and plays essential roles in small RNA production in the germline. Most MUT-7 homologues carry a C-terminal domain of unknown function named MUT7-C appended to the exoribonuclease domain. Our analysis shows that the MUT7-C is evolutionary ancient, as a minimal version of the domain exists as an individual protein in prokaryotes. In animals, MUT7-C has acquired an insertion that diverged during evolution, expanding its functions. Caenorhabditis elegans MUT-7 contains a specific insertion within MUT7-C, which allows binding to MUT-8 and, consequently, MUT-7 recruitment to germ granules. In addition, in C. elegans and human MUT-7, the MUT7-C domain contributes to RNA binding and is thereby crucial for ribonuclease activity. This RNA-binding function most likely represents the ancestral function of the MUT7-C domain. Overall, this study sheds light on MUT7-C and assigns two functions to this previously uncharacterized domain. MUT-7 exoribonuclease activity and localization are mediated by an ancient domain.,Busetto V, Pshanichnaya L, Lichtenberger R, Hann S, Ketting RF, Falk S Nucleic Acids Res. 2024 Aug 27;52(15):9076-9091. doi: 10.1093/nar/gkae610. PMID:39188014[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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