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-Structure paper
タイトル | The structure of the cohesin ATPase elucidates the mechanism of SMC-kleisin ring opening. |
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ジャーナル・号・ページ | Nat Struct Mol Biol, Vol. 27, Issue 3, Page 233-239, Year 2020 |
掲載日 | 2020年2月17日 |
著者 | Kyle W Muir / Yan Li / Felix Weis / Daniel Panne / |
PubMed 要旨 | Genome regulation requires control of chromosome organization by SMC-kleisin complexes. The cohesin complex contains the Smc1 and Smc3 subunits that associate with the kleisin Scc1 to form a ring- ...Genome regulation requires control of chromosome organization by SMC-kleisin complexes. The cohesin complex contains the Smc1 and Smc3 subunits that associate with the kleisin Scc1 to form a ring-shaped complex that can topologically engage chromatin to regulate chromatin structure. Release from chromatin involves opening of the ring at the Smc3-Scc1 interface in a reaction that is controlled by acetylation and engagement of the Smc ATPase head domains. To understand the underlying molecular mechanisms, we have determined the 3.2-Å resolution cryo-electron microscopy structure of the ATPγS-bound, heterotrimeric cohesin ATPase head module and the 2.1-Å resolution crystal structure of a nucleotide-free Smc1-Scc1 subcomplex from Saccharomyces cerevisiae and Chaetomium thermophilium. We found that ATP-binding and Smc1-Smc3 heterodimerization promote conformational changes within the ATPase that are transmitted to the Smc coiled-coil domains. Remodeling of the coiled-coil domain of Smc3 abrogates the binding surface for Scc1, thus leading to ring opening at the Smc3-Scc1 interface. |
リンク | Nat Struct Mol Biol / PubMed:32066964 / PubMed Central |
手法 | EM (単粒子) / X線回折 |
解像度 | 2.1 - 3.3 Å |
構造データ | PDB-6qpq: |
化合物 | ChemComp-HOH: ChemComp-MG: ChemComp-AGS: |
由来 |
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キーワード | CELL CYCLE / Cohesin / cell division / genome regulation / sister chromatid cohesion / SMC / kleisin / Chromatin / genome segregation |