Structure and stability of cohesin's Smc1-kleisin interaction.

@article{Haering2004StructureAS,
  title={Structure and stability of cohesin's Smc1-kleisin interaction.},
  author={Christian H Haering and Doris Schoffnegger and Tatsuya Nishino and Wolfgang Helmhart and Kim Nasmyth and Jan L{\"o}we},
  journal={Molecular cell},
  year={2004},
  volume={15 6},
  pages={
          951-64
        }
}
A multisubunit complex called cohesin forms a huge ring structure that mediates sister chromatid cohesion, possibly by entrapping sister DNAs following replication. Cohesin's kleisin subunit Scc1 completes the ring, connecting the ABC-like ATPase heads of a V-shaped Smc1/3 heterodimer. Proteolytic cleavage of Scc1 by separase triggers sister chromatid disjunction, presumably by breaking the Scc1 bridge. One half of the SMC-kleisin bridge is revealed here by a crystal structure of Smc1's ATPase… CONTINUE READING
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