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Christian H. Haering, Doris Schoffnegger, Tatsuya Nishino, Wolfgang Helmhart, Kim Nasmyth and Jan Löwe
SummaryA multisubunit complex called cohesin forms a huge ring structure that mediates sister chromatid cohesion, possibly by entrapping sister DNAs following replication. Cohesin's kleisin subunit Scc1 completes the ring, connecting the ABC-like ATPase heads of a V-shaped Smc1/3 heterodimer. Proteolytic cleavage of Scc1 by separase triggers sister chromatid disjunction, presumably by breaking the Scc1 bridge. One half of the SMC-kleisin bridge is revealed here by a crystal structure of Smc1's ATPase complexed with Scc1's C-terminal domain. The latter forms a winged helix that binds a pair of β strands in Smc1's ATPase head. Mutation of conserved residues within the contact interface destroys Scc1's interaction with Smc1/3 heterodimers and eliminates cohesin function. Interaction of Scc1's N terminus with Smc3 depends on prior C terminus connection with Smc1. There is little or no turnover of Smc1-Scc1 interactions within cohesin complexes in vivo because expression of noncleavable Scc1 after DNA replication does not hinder anaphase.
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Joseph L Campbell and Orna Cohen-Fix
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Abstract | Full Text | PDF (487 kb) - …more
Copyright © 2002 Cell Press. All rights reserved.
Molecular Cell, Volume 9, Issue 4, 773-788, 1 April 2002
doi:10.1016/S1097-2765(02)00515-4
Article
Molecular Architecture of SMC Proteins and the Yeast Cohesin Complex
Christian H. Haering4, 1, Jan Löwe4, 2, Andreas Hochwagen5, 1 and Kim Nasmyth1, *, 
1 Research Institute of Molecular Pathology, Dr. Bohr Gasse 7, A-1030 Vienna, Austria
2 MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, United Kingdom
Correspondence: Kim Nasmyth, 431 797 30880 (phone), 431 798 9390 (fax)4 These authors contributed equally to this work.
5 Present address: Center for Cancer Research, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139.
Summary
Sister chromatids are held together by the multisubunit cohesin complex, which contains two SMC (Smc1 and Smc3) and two non-SMC (Scc1 and Scc3) proteins. The crystal structure of a bacterial SMC “hinge” region along with EM studies and biochemical experiments on yeast Smc1 and Smc3 proteins show that SMC protamers fold up individually into rod-shaped molecules. A 45 nm long intramolecular coiled coil separates the hinge region from the ATPase-containing “head” domain. Smc1 and Smc3 bind to each other via heterotypic interactions between their hinges to form a V-shaped heterodimer. The two heads of the V-shaped dimer are connected by different ends of the cleavable Scc1 subunit. Cohesin therefore forms a large proteinaceous loop within which sister chromatids might be entrapped after DNA replication.
