Evidence that Loading of Cohesin Onto Chromosomes Involves Opening of Its SMC Hinge

@article{Gruber2006EvidenceTL,
  title={Evidence that Loading of Cohesin Onto Chromosomes Involves Opening of Its SMC Hinge},
  author={Stephan Gruber and Prakash V. Arumugam and Yuki Katou and Daria Kuglitsch and Wolfgang Helmhart and Katsuhiko Shirahige and Kim Nasmyth},
  journal={Cell},
  year={2006},
  volume={127},
  pages={523-537}
}
Cohesin is a multisubunit complex that mediates sister-chromatid cohesion. Its Smc1 and Smc3 subunits possess ABC-like ATPases at one end of 50 nm long coiled coils. At the other ends are pseudosymmetrical hinge domains that interact to create V-shaped Smc1/Smc3 heterodimers. N- and C-terminal domains within cohesin's kleisin subunit Scc1 bind to Smc3 and Smc1 ATPase heads respectively, thereby creating a huge tripartite ring. It has been suggested that cohesin associates with chromosomes by… CONTINUE READING
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