Closing the cohesin ring: structure and function of its Smc3-kleisin interface

Gligoris, Thomas G, Scheinost, Johanna C, Bürmann, Frank, Petela, Naomi, Chan, Kok-Lung, Uluocak, Pelin, Beckouët, Frédéric, Gruber, Stephan, Nasmyth, Kim and Löwe, Jan (2014) Closing the cohesin ring: structure and function of its Smc3-kleisin interface. Science, 346 (6212). pp. 963-967. ISSN 1095-9203

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Through their association with a kleisin subunit (Scc1), cohesin’s Smc1 and Smc3 subunits
are thought to form tripartite rings that mediate sister chromatid cohesion. Unlike the
structure of Smc1/Smc3 and Smc1/Scc1 interfaces, that of Smc3/Scc1 is not known.
Disconnection of this interface is thought to release cohesin from chromosomes in a
process regulated by acetylation. We show here that the N-terminal domain of yeast Scc1
contains two a helices, forming a four-helix bundle with the coiled coil emerging from
Smc3’s adenosine triphosphatase head. Mutations affecting this interaction compromise
cohesin’s association with chromosomes. The interface is far from Smc3 residues,
whose acetylation prevents cohesin’s dissociation from chromosomes. Cohesin complexes
holding chromatids together in vivo do indeed have the configuration of hetero-trimeric
rings, and sister DNAs are entrapped within these.

Item Type: Article
Schools and Departments: School of Life Sciences > Sussex Centre for Genome Damage and Stability
Subjects: Q Science > QD Chemistry > QD0241 Organic chemistry > QD0415 Biochemistry
Depositing User: Gee Wheatley
Date Deposited: 20 Jan 2015 12:15
Last Modified: 23 Jul 2020 09:49

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