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

• Published in: Science (American Association for the Advancement of Science) Vol. 346; no. 6212; pp. 963 - 967
• Main Authors: Gligoris, Thomas G., Scheinost, Johanna C., Bürmann, Frank, Petela, Naomi, Chan, Kok-Lung, Uluocak, Pelin, Beckouët, Frédéric, Gruber, Stephan, Nasmyth, Kim, Löwe, Jan
• Format: Journal Article
• Language: English
• Published: United States American Association for the Advancement of Science 21.11.2014; The American Association for the Advancement of Science
• Subjects: Acetylation; Adenosine triphosphatase; Adenosine triphosphatases; Adenosine Triphosphatases - chemistry; adenosinetriphosphatase; Amino Acid Sequence; Bundling; Cell Cycle Proteins - chemistry; Cell Cycle Proteins - genetics; Chromatids; Chromatin; Chromosomal Proteins, Non-Histone - chemistry; Chromosomal Proteins, Non-Histone - genetics; Chromosomes; Circles; Cohesins; Cohesion; Coiling; Conserved Sequence; Cross-Linking Reagents - chemistry; Crystal structure; Crystallography, X-Ray; Deoxyribonucleic acid; Dimers; dissociation; DNA; DNA - chemistry; Immunoprecipitation; Mathematical rings; Molecules; Mutation; Mutations; Protein Multimerization; Protein Structure, Tertiary; Saccharomyces cerevisiae Proteins - chemistry; Saccharomyces cerevisiae Proteins - genetics; Strands; Yeast; Yeasts

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 t...