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| | ==Structure of Csm1 C-terminal domain, P21212 form== | | ==Structure of Csm1 C-terminal domain, P21212 form== |
| - | <StructureSection load='3n4s' size='340' side='right' caption='[[3n4s]], [[Resolution|resolution]] 2.35Å' scene=''> | + | <StructureSection load='3n4s' size='340' side='right'caption='[[3n4s]], [[Resolution|resolution]] 2.35Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3n4s]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3N4S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3N4S FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3n4s]] is a 4 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=3N4S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3N4S FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</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]] 2.35Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3n4r|3n4r]], [[3n4x|3n4x]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CSM1, SPO86, YCR086W, YCR86W ([http://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=3n4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n4s OCA], [https://pdbe.org/3n4s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3n4s RCSB], [https://www.ebi.ac.uk/pdbsum/3n4s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3n4s 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=3n4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n4s OCA], [http://pdbe.org/3n4s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3n4s RCSB], [http://www.ebi.ac.uk/pdbsum/3n4s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3n4s ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CSM1_YEAST CSM1_YEAST]] Component of the monopolin complex which promotes monoorientation during meiosis I, required for chromosome segregation during meiosis. Plays also a mitotic role in DNA replication.<ref>PMID:11470404</ref> <ref>PMID:12689592</ref> <ref>PMID:15023545</ref> <ref>PMID:16487579</ref> <ref>PMID:18997772</ref> | + | [https://www.uniprot.org/uniprot/CSM1_YEAST CSM1_YEAST] Component of the monopolin complex which promotes monoorientation during meiosis I, required for chromosome segregation during meiosis. Plays also a mitotic role in DNA replication.<ref>PMID:11470404</ref> <ref>PMID:12689592</ref> <ref>PMID:15023545</ref> <ref>PMID:16487579</ref> <ref>PMID:18997772</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/n4/3n4s_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/n4/3n4s_consurf.spt"</scriptWhenChecked> |
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 18824]] | + | [[Category: Large Structures]] |
| - | [[Category: Corbett, K D]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Harrison, S C]] | + | [[Category: Corbett KD]] |
| - | [[Category: Meiosis]] | + | [[Category: Harrison SC]] |
| - | [[Category: Rdna]]
| + | |
| - | [[Category: Replication]]
| + | |
| Structural highlights
Function
CSM1_YEAST Component of the monopolin complex which promotes monoorientation during meiosis I, required for chromosome segregation during meiosis. Plays also a mitotic role in DNA replication.[1] [2] [3] [4] [5]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The monopolin complex regulates different types of kinetochore-microtubule attachments in fungi, ensuring sister chromatid co-orientation in Saccharomyces cerevisiae meiosis I and inhibiting merotelic attachment in Schizosaccharomyces pombe mitosis. In addition, the monopolin complex maintains the integrity and silencing of ribosomal DNA (rDNA) repeats in the nucleolus. We show here that the S. cerevisiae Csm1/Lrs4 monopolin subcomplex has a distinctive V-shaped structure, with two pairs of protein-protein interaction domains positioned approximately 10 nm apart. Csm1 presents a conserved hydrophobic surface patch that binds two kinetochore proteins: Dsn1, a subunit of the outer-kinetochore MIND/Mis12 complex, and Mif2/CENP-C. Csm1 point-mutations that disrupt kinetochore-subunit binding also disrupt sister chromatid co-orientation in S. cerevisiae meiosis I. We further show that the same Csm1 point-mutations affect rDNA silencing, probably by disrupting binding to the rDNA-associated protein Tof2. We propose that Csm1/Lrs4 functions as a molecular clamp, crosslinking kinetochore components to enforce sister chromatid co-orientation in S. cerevisiae meiosis I and to suppress merotelic attachment in S. pombe mitosis, and crosslinking rDNA repeats to aid rDNA silencing.
The monopolin complex crosslinks kinetochore components to regulate chromosome-microtubule attachments.,Corbett KD, Yip CK, Ee LS, Walz T, Amon A, Harrison SC Cell. 2010 Aug 20;142(4):556-67. PMID:20723757[6]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Rabitsch KP, Toth A, Galova M, Schleiffer A, Schaffner G, Aigner E, Rupp C, Penkner AM, Moreno-Borchart AC, Primig M, Esposito RE, Klein F, Knop M, Nasmyth K. A screen for genes required for meiosis and spore formation based on whole-genome expression. Curr Biol. 2001 Jul 10;11(13):1001-9. PMID:11470404
- ↑ Rabitsch KP, Petronczki M, Javerzat JP, Genier S, Chwalla B, Schleiffer A, Tanaka TU, Nasmyth K. Kinetochore recruitment of two nucleolar proteins is required for homolog segregation in meiosis I. Dev Cell. 2003 Apr;4(4):535-48. PMID:12689592
- ↑ Wysocka M, Rytka J, Kurlandzka A. Saccharomyces cerevisiae CSM1 gene encoding a protein influencing chromosome segregation in meiosis I interacts with elements of the DNA replication complex. Exp Cell Res. 2004 Apr 1;294(2):592-602. PMID:15023545 doi:10.1016/j.yexcr.2003.12.008
- ↑ Pan X, Ye P, Yuan DS, Wang X, Bader JS, Boeke JD. A DNA integrity network in the yeast Saccharomyces cerevisiae. Cell. 2006 Mar 10;124(5):1069-81. Epub 2006 Feb 16. PMID:16487579 doi:S0092-8674(06)00118-8
- ↑ Mekhail K, Seebacher J, Gygi SP, Moazed D. Role for perinuclear chromosome tethering in maintenance of genome stability. Nature. 2008 Dec 4;456(7222):667-70. doi: 10.1038/nature07460. Epub 2008 Nov 9. PMID:18997772 doi:10.1038/nature07460
- ↑ Corbett KD, Yip CK, Ee LS, Walz T, Amon A, Harrison SC. The monopolin complex crosslinks kinetochore components to regulate chromosome-microtubule attachments. Cell. 2010 Aug 20;142(4):556-67. PMID:20723757 doi:10.1016/j.cell.2010.07.017
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