Research Article

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

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Science  21 Nov 2014:
Vol. 346, Issue 6212, pp. 963-967
DOI: 10.1126/science.1256917

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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 α 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.

A cohesin ring around two DNA strands

Holding together homologous sister chromosome pairs is a vital requirement during cell division and DNA repair. A special complex, called cohesin, forms a ring made of three different proteins and functions to hold together the two sister DNA strands. Gligoris et al. and Huis in 't Veld et al. identified a specific protein-protein interface within the cohesin ring that forms a DNA exit gate. Mutations in this interface prevented cohesion between sister chromatids. Thus, the cohesin ring must indeed encircle the two DNA strands to hold them together.

Science, this issue p. 963, p. 968

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