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| | <SX load='3izq' size='340' side='right' viewer='molstar' caption='[[3izq]], [[Resolution|resolution]] 9.50Å' scene=''> | | <SX load='3izq' size='340' side='right' viewer='molstar' caption='[[3izq]], [[Resolution|resolution]] 9.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3izq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IZQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IZQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3izq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IZQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IZQ FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3ize|3ize]], [[3izf|3izf]], [[3izb|3izb]], [[3izc|3izc]]</div></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 9.5Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DOM34, N2016, YNL001W ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824]), HBS1, YKR084C, YKR404 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=3izq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3izq OCA], [https://pdbe.org/3izq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3izq RCSB], [https://www.ebi.ac.uk/pdbsum/3izq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3izq ProSAT]</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=3izq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3izq OCA], [https://pdbe.org/3izq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3izq RCSB], [https://www.ebi.ac.uk/pdbsum/3izq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3izq ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/DOM34_YEAST DOM34_YEAST]] Involved in protein translation. Together with HBS1, may function in recognizing stalled ribosomes and triggering endonucleolytic cleavage of the mRNA, a mechanism to release non-functional ribosomes and degrade damaged mRNAs. The complex formed by DOM34 and HBS1 has ribonuclease activity towards double-stranded RNA substrates, but does not cleave single-stranded RNA. Acts as endonuclease; has no exonuclease activity. Increases the affinity of HBS1 for GTP, but nor for GDP. Promotes G1 progression and differentiation and is involved in mitotic and meiotic cell divisions.<ref>PMID:16554824</ref> <ref>PMID:17889667</ref> <ref>PMID:18180287</ref> [[https://www.uniprot.org/uniprot/HBS1_YEAST HBS1_YEAST]] Involved in protein translation. Together with DOM34, may function in recognizing stalled ribosomes and triggering endonucleolytic cleavage of the mRNA, a mechanism to release non-functional ribosomes and degrade damaged mRNAs.<ref>PMID:16554824</ref>
| + | [https://www.uniprot.org/uniprot/DOM34_YEAST DOM34_YEAST] Involved in protein translation. Together with HBS1, may function in recognizing stalled ribosomes and triggering endonucleolytic cleavage of the mRNA, a mechanism to release non-functional ribosomes and degrade damaged mRNAs. The complex formed by DOM34 and HBS1 has ribonuclease activity towards double-stranded RNA substrates, but does not cleave single-stranded RNA. Acts as endonuclease; has no exonuclease activity. Increases the affinity of HBS1 for GTP, but nor for GDP. Promotes G1 progression and differentiation and is involved in mitotic and meiotic cell divisions.<ref>PMID:16554824</ref> <ref>PMID:17889667</ref> <ref>PMID:18180287</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </SX> | | </SX> |
| - | [[Category: Atcc 18824]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Anger, A M]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Armache, J P]] | + | [[Category: Abdel Motaal B]] |
| - | [[Category: Becker, T]] | + | [[Category: Anger AM]] |
| - | [[Category: Beckmann, R]] | + | [[Category: Armache J-P]] |
| - | [[Category: Berninghausen, O]] | + | [[Category: Becker T]] |
| - | [[Category: Jarasch, A]] | + | [[Category: Beckmann R]] |
| - | [[Category: Mielke, T]] | + | [[Category: Berninghausen O]] |
| - | [[Category: Motaal, B Abdel]]
| + | [[Category: Jarasch A]] |
| - | [[Category: Sieber, H]] | + | [[Category: Mielke T]] |
| - | [[Category: Villa, E]] | + | [[Category: Sieber H]] |
| - | [[Category: Hydrolase]]
| + | [[Category: Villa E]] |
| - | [[Category: No-go mrna decay]]
| + | |
| - | [[Category: Ribosomal protein]]
| + | |
| Structural highlights
Function
DOM34_YEAST Involved in protein translation. Together with HBS1, may function in recognizing stalled ribosomes and triggering endonucleolytic cleavage of the mRNA, a mechanism to release non-functional ribosomes and degrade damaged mRNAs. The complex formed by DOM34 and HBS1 has ribonuclease activity towards double-stranded RNA substrates, but does not cleave single-stranded RNA. Acts as endonuclease; has no exonuclease activity. Increases the affinity of HBS1 for GTP, but nor for GDP. Promotes G1 progression and differentiation and is involved in mitotic and meiotic cell divisions.[1] [2] [3]
Publication Abstract from PubMed
No-go decay (NGD) is a mRNA quality-control mechanism in eukaryotic cells that leads to degradation of mRNAs stalled during translational elongation. The key factors triggering NGD are Dom34 and Hbs1. We used cryo-EM to visualize NGD intermediates resulting from binding of the Dom34-Hbs1 complex to stalled ribosomes. At subnanometer resolution, all domains of Dom34 and Hbs1 were identified, allowing the docking of crystal structures and homology models. Moreover, the close structural similarity of Dom34 and Hbs1 to eukaryotic release factors (eRFs) enabled us to propose a model for the ribosome-bound eRF1-eRF3 complex. Collectively, our data provide structural insights into how stalled mRNA is recognized on the ribosome and how the eRF complex can simultaneously recognize stop codons and catalyze peptide release.
Structure of the no-go mRNA decay complex Dom34-Hbs1 bound to a stalled 80S ribosome.,Becker T, Armache JP, Jarasch A, Anger AM, Villa E, Sieber H, Motaal BA, Mielke T, Berninghausen O, Beckmann R Nat Struct Mol Biol. 2011 Jun;18(6):715-20. Epub 2011 May 29. PMID:21623367[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Doma MK, Parker R. Endonucleolytic cleavage of eukaryotic mRNAs with stalls in translation elongation. Nature. 2006 Mar 23;440(7083):561-4. PMID:16554824 doi:nature04530
- ↑ Lee HH, Kim YS, Kim KH, Heo I, Kim SK, Kim O, Kim HK, Yoon JY, Kim HS, Kim do J, Lee SJ, Yoon HJ, Kim SJ, Lee BG, Song HK, Kim VN, Park CM, Suh SW. Structural and functional insights into Dom34, a key component of no-go mRNA decay. Mol Cell. 2007 Sep 21;27(6):938-50. PMID:17889667 doi:10.1016/j.molcel.2007.07.019
- ↑ Graille M, Chaillet M, van Tilbeurgh H. Structure of yeast Dom34: a protein related to translation termination factor Erf1 and involved in No-Go decay. J Biol Chem. 2008 Mar 14;283(11):7145-54. Epub 2008 Jan 7. PMID:18180287 doi:10.1074/jbc.M708224200
- ↑ Becker T, Armache JP, Jarasch A, Anger AM, Villa E, Sieber H, Motaal BA, Mielke T, Berninghausen O, Beckmann R. Structure of the no-go mRNA decay complex Dom34-Hbs1 bound to a stalled 80S ribosome. Nat Struct Mol Biol. 2011 Jun;18(6):715-20. Epub 2011 May 29. PMID:21623367 doi:10.1038/nsmb.2057
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