Cookies on this website

We use cookies to ensure that we give you the best experience on our website. If you click 'Accept all cookies' we'll assume that you are happy to receive all cookies and you won't see this message again. If you click 'Reject all non-essential cookies' only necessary cookies providing core functionality such as security, network management, and accessibility will be enabled. Click 'Find out more' for information on how to change your cookie settings.

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.


Journal article


Mol Cell

Publication Date





773 - 788


Adenosine Triphosphatases, Bacterial Proteins, Cell Cycle Proteins, Chondroitin Sulfate Proteoglycans, Chromatids, Chromosomal Proteins, Non-Histone, DNA Replication, Dimerization, Eukaryotic Cells, Fungal Proteins, Macromolecular Substances, Models, Biological, Models, Molecular, Nuclear Proteins, Phosphoproteins, Prokaryotic Cells, Protein Binding, Protein Conformation, Protein Interaction Mapping, Protein Structure, Tertiary, Protein Subunits, Recombinant Fusion Proteins, Saccharomyces cerevisiae Proteins, Structure-Activity Relationship, Thermotoga maritima, X-Ray Diffraction