Scc2 Is a Potent Activator of Cohesin’s ATPase that Promotes Loading by Binding Scc1 without Pds5

@inproceedings{Petela2018Scc2IA,
  title={Scc2 Is a Potent Activator of Cohesin’s ATPase that Promotes Loading by Binding Scc1 without Pds5},
  author={Naomi J. Petela and Thomas G. Gligoris and Jean Metson and Byung-Gil Lee and Menelaos Voulgaris and Bin Hu and Sotaro Kikuchi and Christophe Chapard and Wentao Chen and Eeson Rajendra and Madhusudhan Srinivisan and Hongtao Yu and Jan L{\"o}we and Kim A Nasmyth},
  booktitle={Molecular cell},
  year={2018}
}
Cohesin organizes DNA into chromatids, regulates enhancer-promoter interactions, and confers sister chromatid cohesion. Its association with chromosomes is regulated by hook-shaped HEAT repeat proteins that bind Scc1, namely Scc3, Pds5, and Scc2. Unlike Pds5, Scc2 is not a stable cohesin constituent but, as shown here, transiently replaces Pds5. Scc1 mutations that compromise its interaction with Scc2 adversely affect cohesin's ATPase activity and loading. Moreover, Scc2 mutations that alter… CONTINUE READING
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