ATP Hydrolysis Is Required for Relocating Cohesin from Sites Occupied by Its Scc2/4 Loading Complex

@article{Hu2011ATPHI,
  title={ATP Hydrolysis Is Required for Relocating Cohesin from Sites Occupied by Its Scc2/4 Loading Complex},
  author={Bin Hu and Takehiko Itoh and Ajay Mishra and Yuki Katoh and Kok-Lung Chan and William R. Upcher and Camilla Godlee and Maurici Brunet Roig and Katsuhiko Shirahige and Kim Nasmyth},
  journal={Current Biology},
  year={2011},
  volume={21},
  pages={12-24}
}
BACKGROUND The Cohesin complex that holds sister chromatins together until anaphase is comprised of three core subunits: Smc1 and Smc3, two long-rod-shaped proteins with an ABC-like ATPase head (nucleotide-binding domain [NBD]) and a dimerization domain linked by a 50 nm long intramolecular antiparallel coiled-coil, and Scc1, an α-kleisin subunit interconnecting the NBD domains of Smc1 and Smc3. Cohesin's stable association with chromosomes is thought to involve entrapment of chromatin fibers… CONTINUE READING
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