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Releasing activity disengages Cohesin’s Smc3/Scc1 interface in a process blocked by Acetylation

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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 Nasmyth
Sister 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 Cell

ISSN

1097-2765

Publisher

Elsevier

Issue

4

Volume

61

Page range

563-574

Department affiliated with

  • Sussex Centre for Genome Damage Stability Publications

Full text available

  • Yes

Peer reviewed?

  • Yes

Legacy Posted Date

2016-05-18

First Open Access (FOA) Date

2016-05-18

First Compliant Deposit (FCD) Date

2016-05-18

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