Structure and function of cohesin’s Scc3/SA regulatory subunit |
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Authors: | Maurici B Roig Jan Löwe Kok-Lung Chan Frédéric Beckouët Jean Metson Kim Nasmyth |
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Institution: | 1. Department of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom;2. MRC Laboratory of Molecular Biology, Structural Studies Division, Francis Crick Avenue, Cambridge CB2 0QH, United Kingdom |
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Abstract: | Sister chromatid cohesion involves entrapment of sister DNAs by a cohesin ring created through association of a kleisin subunit (Scc1) with ATPase heads of Smc1/Smc3 heterodimers. Cohesin’s association with chromatin involves subunits recruited by Scc1: Wapl, Pds5, and Scc3/SA, in addition to Scc2/4 loading complex. Unlike Pds5, Wapl, and Scc2/4, Scc3s are encoded by all eukaryotic genomes. Here, a crystal structure of Scc3 reveals a hook-shaped protein composed of tandem α helices. Its N-terminal domain contains a conserved and essential surface (CES) present even in organisms lacking Pds5, Wapl, and Scc2/4, while its C-terminal domain binds a section of the kleisin Scc1. Scc3 turns over in G2/M while maintaining cohesin’s association with chromosomes and it promotes de-acetylation of Smc3 upon Scc1 cleavage. |
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Keywords: | Scc3 SA/STAG domain Eco1 acetylation Releasing activity Cohesin complex Sister chromatid separation Maintenance of cohesion Smc proteins |
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