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Releasing activity disengages Cohesin’s Smc3/Scc1 interface in a process blocked by Acetylation
journal contribution
posted on 2023-06-09, 01:18 authored by Frederick Beckouët, Madhusudhan Srinivasan, Maurici Brunet Roig, Kok-Lung ChanKok-Lung Chan, Johanna C Scheinost, Paul Batty, Bin Hu, Naomi Petela, Thomas Gligoris, Alexandra C Smith, Lana Strmecki, Benjamin D Rowland, Kim NasmythSister chromatid cohesion conferred by entrapment of sister DNAs within a tripartite ring formed between cohesin’s Scc1, Smc1, and Smc3 subunits is created during S and destroyed at anaphase through Scc1 cleavage by separase. Cohesin’s association with chromosomes is controlled by opposing activities: loading by Scc2/4 complex and release by a separase- independent releasing activity as well as by cleavage. Coentrapment of sister DNAs at replication is accompanied by acetylation of Smc3 by Eco1, which blocks releasing activity and ensures that sisters remain connected. Because fusion of Smc3 to Scc1 prevents release and bypasses the requirement for Eco1, we suggested that release is mediated by disengagement of the Smc3/Scc1 interface. We show that mutations capable of bypassing Eco1 in Smc1, Smc3, Scc1, Wapl, Pds5, and Scc3 subunits reduce dissociation of N-terminal cleavage fragments of Scc1 (NScc1) from Smc3. This process involves interaction between Smc ATPase heads and is inhibited by Smc3 acetylation.
History
Publication status
- Published
File Version
- Published version
Journal
Molecular CellISSN
1097-2765Publisher
ElsevierExternal DOI
Issue
4Volume
61Page range
563-574Department affiliated with
- Sussex Centre for Genome Damage Stability Publications
Full text available
- Yes
Peer reviewed?
- Yes
Legacy Posted Date
2016-05-18First Open Access (FOA) Date
2016-05-18First Compliant Deposit (FCD) Date
2016-05-18Usage metrics
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