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    Mol Cell. 2002 Apr;9(4):773-88.

    Molecular architecture of SMC proteins and the yeast cohesin complex.

    Haering CH, Löwe J, Hochwagen A, Nasmyth K.

    Source

    Research Institute of Molecular Pathology, Dr. Bohr Gasse 7, A-1030 Vienna, Austria.

    Abstract

    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.

    PMID:
    11983169
    [PubMed - indexed for MEDLINE]

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