Cohesin's ATPase Activity Is Stimulated by the C-Terminal Winged-Helix Domain of Its Kleisin Subunit

@article{Arumugam2006CohesinsAA,
  title={Cohesin's ATPase Activity Is Stimulated by the C-Terminal Winged-Helix Domain of Its Kleisin Subunit},
  author={Prakash Arumugam and Tatsuya Nishino and Christian H Haering and Stephan Gruber and Kim Nasmyth},
  journal={Current Biology},
  year={2006},
  volume={16},
  pages={1998-2008}
}
BACKGROUND Cohesin, a multisubunit protein complex conserved from yeast to humans, holds sister chromatids together from the onset of replication to their separation during anaphase. Cohesin consists of four core subunits, namely Smc1, Smc3, Scc1, and Scc3. Smc1 and Smc3 proteins are characterized by 50-nm-long anti-parallel coiled coils flanked by a globular hinge domain and an ABC-like ATPase head domain. Whereas Smc1 and Smc3 heterodimerize via their hinge domains, the kleisin subunit Scc1… CONTINUE READING
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