Journal
FEBS LETTERS
Volume 588, Issue 20, Pages 3692-3702Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2014.08.015
Keywords
Scc3; SA/STAG domain; Eco1 acetylation; Releasing activity; Cohesin complex; Sister chromatid separation; Maintenance of cohesion; Smc proteins
Funding
- Medical Research Council [U10518432]
- Wellcome Trust [095514/Z/11/Z, 091859/Z/10/Z]
- Cancer Research UK [C573/A 12386]
- MRC [MC_U105184326] Funding Source: UKRI
- Wellcome Trust [091859/Z/10/Z] Funding Source: Wellcome Trust
- Cancer Research UK [12386] Funding Source: researchfish
- Medical Research Council [MC_U105184326] Funding Source: researchfish
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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 a 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. (C) 2014 The Authors. Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.
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