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| - | {{STRUCTURE_4c8q| PDB=4c8q | SCENE= }} | |
| - | ===Crystal structure of the yeast Lsm1-7-Pat1 complex=== | |
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| - | ==Function== | + | ==Crystal structure of the yeast Lsm1-7-Pat1 complex== |
| - | [[http://www.uniprot.org/uniprot/LSM3_YEAST LSM3_YEAST]] Component of LSm protein complexes, which are involved in RNA processing and may function in a chaperone-like manner. Component of the cytoplasmic LSM1-LSM7 complex which is thought to be involved in mRNA degradation by activating the decapping step. Component of the nuclear LSM2-LSM8 complex, which is involved in splicing of nuclear mRNAs. LSM2-LSM8 associates with multiple snRNP complexes containing the U6 snRNA (U4/U6 snRNP, U4/U6.U5 snRNP, and free U6 snRNP). It binds directly to the U6 snRNA and plays a role in the biogenesis and stability of the U6 snRNP and U4/U6 snRNP complexes. It probably also is involved degradation of nuclear pre-mRNA by targeting them for decapping. LSM3 binds specifically to the 3'-terminal U-tract of U6 snRNA. LSM2-LSM8 probably is involved in processing of pre-tRNAs, pre-rRNAs and U3 snoRNA. LSM3, probably in a complex that contains LSM2-LSM7 but not LSM1 or LSM8, associates with the precursor of the RNA component of RNase P (pre-P RNA) and may be involved in maturing pre-P RNA. LSM3 is required for processing of pre-tRNAs, pre-rRNAs and U3 snoRNA.<ref>PMID:7744014</ref> <ref>PMID:10747033</ref> <ref>PMID:10761922</ref> <ref>PMID:12077351</ref> <ref>PMID:12438310</ref> <ref>PMID:15485930</ref> [[http://www.uniprot.org/uniprot/PAT1_YEAST PAT1_YEAST]] Activator of decapping that functions as a general and active mechanism of translational repression and required for P-body formation. First decay factor recruited to mRNA, at a time when the mRNA is still associated with translation factors. Subsequently, PAT1 recruits the hepta-heterodimer LSM1-LSM7 complex to P-bodies. In association with the LSM1-LSM7 complex, stabilizes the 3' terminus of mRNAs. This association is also required for mosaic virus genomic RNA translation. Modulates the rates of mRNA-decapping that occur following deadenylation. Might be required for promoting the formation or the stabilization of the preinitiation translation complexes. Required for 40S ribosomal subunit joining to capped and/or polyadenylated mRNA. With other P-body components, enhances the formation of retrotransposition-competent Ty1 virus-like particles. Necessary for accurate chromosome transmission during cell division.<ref>PMID:8816497</ref> <ref>PMID:8972867</ref> <ref>PMID:10523645</ref> <ref>PMID:10394921</ref> <ref>PMID:10747033</ref> <ref>PMID:10779343</ref> <ref>PMID:10913177</ref> <ref>PMID:11027264</ref> <ref>PMID:10761922</ref> <ref>PMID:11514438</ref> <ref>PMID:12773554</ref> <ref>PMID:16179257</ref> <ref>PMID:17875743</ref> <ref>PMID:17429074</ref> <ref>PMID:17513695</ref> <ref>PMID:18086885</ref> <ref>PMID:19901074</ref> <ref>PMID:20832728</ref> | + | <StructureSection load='4c8q' size='340' side='right'caption='[[4c8q]], [[Resolution|resolution]] 3.70Å' scene=''> |
| | + | == Structural highlights == |
| | + | <table><tr><td colspan='2'>[[4c8q]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C8Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C8Q 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]] 3.698Å</td></tr> |
| | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</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=4c8q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c8q OCA], [https://pdbe.org/4c8q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c8q RCSB], [https://www.ebi.ac.uk/pdbsum/4c8q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c8q ProSAT]</span></td></tr> |
| | + | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/LSM1_YEAST LSM1_YEAST] Component of the cytoplasmic LSM1-LSM7 complex which is involved in mRNA degradation by activating the decapping step.<ref>PMID:10747033</ref> <ref>PMID:10913177</ref> <ref>PMID:10761922</ref> |
| | + | <div style="background-color:#fffaf0;"> |
| | + | == Publication Abstract from PubMed == |
| | + | The decay of mRNAs is a key step in eukaryotic gene expression. The cytoplasmic Lsm1-7-Pat1 complex is a conserved component of the 5'-to-3' mRNA decay pathway, linking deadenylation to decapping. Lsm1-7 is similar to the nuclear Sm complexes that bind oligo-uridine tracts in snRNAs. The 2.3 A resolution structure of S. cerevisiae Lsm1-7 shows the presence of a heptameric ring with Lsm1-2-3-6-5-7-4 topology. A distinct structural feature of the cytoplasmic Lsm ring is the C-terminal extension of Lsm1, which plugs the exit site of the central channel and approaches the RNA binding pockets. The 3.7 A resolution structure of Lsm1-7 bound to the C-terminal domain of Pat1 reveals that Pat1 recognition is not mediated by the distinguishing cytoplasmic subunit, Lsm1, but by Lsm2 and Lsm3. These results show how the auxiliary domains and the canonical Sm folds of the Lsm1-7 complex are organized in order to mediate and modulate macromolecular interactions. |
| | | | |
| - | ==About this Structure==
| + | Architecture of the Lsm1-7-Pat1 Complex: A Conserved Assembly in Eukaryotic mRNA Turnover.,Sharif H, Conti E Cell Rep. 2013 Oct 15. pii: S2211-1247(13)00573-1. doi:, 10.1016/j.celrep.2013.10.004. PMID:24139796<ref>PMID:24139796</ref> |
| - | [[4c8q]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Clostridium_acetobutylicum Clostridium acetobutylicum], [http://en.wikipedia.org/wiki/Rhizobium_loessense Rhizobium loessense] and [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_s288c Saccharomyces cerevisiae s288c]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C8Q OCA].
| + | |
| | | | |
| - | ==Reference==
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | <references group="xtra"/><references/> | + | </div> |
| - | [[Category: Clostridium acetobutylicum]] | + | <div class="pdbe-citations 4c8q" style="background-color:#fffaf0;"></div> |
| - | [[Category: Rhizobium loessense]] | + | |
| - | [[Category: Saccharomyces cerevisiae s288c]] | + | ==See Also== |
| - | [[Category: Conti, E.]] | + | *[[Sm-like protein 3D structures|Sm-like protein 3D structures]] |
| - | [[Category: Sharif, H.]] | + | == References == |
| - | [[Category: Mrna decapping]]
| + | <references/> |
| - | [[Category: Mrna degradation]]
| + | __TOC__ |
| - | [[Category: Sm fold]]
| + | </StructureSection> |
| - | [[Category: Transcription]]
| + | [[Category: Large Structures]] |
| | + | [[Category: Saccharomyces cerevisiae S288C]] |
| | + | [[Category: Conti E]] |
| | + | [[Category: Sharif H]] |
| Structural highlights
Function
LSM1_YEAST Component of the cytoplasmic LSM1-LSM7 complex which is involved in mRNA degradation by activating the decapping step.[1] [2] [3]
Publication Abstract from PubMed
The decay of mRNAs is a key step in eukaryotic gene expression. The cytoplasmic Lsm1-7-Pat1 complex is a conserved component of the 5'-to-3' mRNA decay pathway, linking deadenylation to decapping. Lsm1-7 is similar to the nuclear Sm complexes that bind oligo-uridine tracts in snRNAs. The 2.3 A resolution structure of S. cerevisiae Lsm1-7 shows the presence of a heptameric ring with Lsm1-2-3-6-5-7-4 topology. A distinct structural feature of the cytoplasmic Lsm ring is the C-terminal extension of Lsm1, which plugs the exit site of the central channel and approaches the RNA binding pockets. The 3.7 A resolution structure of Lsm1-7 bound to the C-terminal domain of Pat1 reveals that Pat1 recognition is not mediated by the distinguishing cytoplasmic subunit, Lsm1, but by Lsm2 and Lsm3. These results show how the auxiliary domains and the canonical Sm folds of the Lsm1-7 complex are organized in order to mediate and modulate macromolecular interactions.
Architecture of the Lsm1-7-Pat1 Complex: A Conserved Assembly in Eukaryotic mRNA Turnover.,Sharif H, Conti E Cell Rep. 2013 Oct 15. pii: S2211-1247(13)00573-1. doi:, 10.1016/j.celrep.2013.10.004. PMID:24139796[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Bouveret E, Rigaut G, Shevchenko A, Wilm M, Seraphin B. A Sm-like protein complex that participates in mRNA degradation. EMBO J. 2000 Apr 3;19(7):1661-71. PMID:10747033 doi:10.1093/emboj/19.7.1661
- ↑ Bonnerot C, Boeck R, Lapeyre B. The two proteins Pat1p (Mrt1p) and Spb8p interact in vivo, are required for mRNA decay, and are functionally linked to Pab1p. Mol Cell Biol. 2000 Aug;20(16):5939-46. PMID:10913177
- ↑ Tharun S, He W, Mayes AE, Lennertz P, Beggs JD, Parker R. Yeast Sm-like proteins function in mRNA decapping and decay. Nature. 2000 Mar 30;404(6777):515-8. PMID:10761922 doi:10.1038/35006676
- ↑ Sharif H, Conti E. Architecture of the Lsm1-7-Pat1 Complex: A Conserved Assembly in Eukaryotic mRNA Turnover. Cell Rep. 2013 Oct 15. pii: S2211-1247(13)00573-1. doi:, 10.1016/j.celrep.2013.10.004. PMID:24139796 doi:http://dx.doi.org/10.1016/j.celrep.2013.10.004
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