Releasing Activity Disengages Cohesin’s Smc3/Scc1 Interface in a Process Blocked by Acetylation

Frederic Beckouët, Madhusudhan Srinivasan, Maurici Brunet Roig, Kok-Lung Chan, Johanna C. Scheinost, Paul Batty, Bin Hu, Naomi Petela, Thomas Gligoris, Alexandra C. Smith, Lana Strmecki, Benjamin D. Rowland , Kim Nasmyth*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

76 Citations (Scopus)
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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.
Original languageEnglish
Pages (from-to)563-574
Number of pages13
JournalMolecular Cell
Issue number4
Early online date18 Feb 2016
Publication statusPublished - 18 Feb 2016
Externally publishedYes

Bibliographical note

We are grateful to K. Shirahige for supplying anti-acetylated Smc3 antibody
and to all members of the Nasmyth group for valuable discussions. This
work was funded by the Wellcome Trust (091859/Z/10/Z to K.N.) and Cancer
Research UK (C573/A 12386 to K.N.).


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