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

Beckouët, Frederick, Srinivasan, Madhusudhan, Brunet Roig, Maurici, Chan, Kok-Lung, Scheinost, Johanna C, Batty, Paul, Hu, Bin, Petela, Naomi, Gligoris, Thomas, Smith, Alexandra C, Strmecki, Lana, Rowland, Benjamin D and Nasmyth, Kim (2016) Releasing activity disengages Cohesin’s Smc3/Scc1 interface in a process blocked by Acetylation. Molecular Cell, 61 (4). pp. 563-574. ISSN 1097-2765

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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.

Item Type: Article
Schools and Departments: School of Life Sciences > Sussex Centre for Genome Damage and Stability
Depositing User: Gee Wheatley
Date Deposited: 18 May 2016 11:29
Last Modified: 25 Sep 2020 17:34

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