Cohesin’s ATPase Activity Couples Cohesin Loading onto DNA with Smc3 Acetylation

@inproceedings{Ladurner2014CohesinsAA,
  title={Cohesin’s ATPase Activity Couples Cohesin Loading onto DNA with Smc3 Acetylation},
  author={Rene Ladurner and Venugopal Bhaskara and Pim J. Huis in ’t Veld and Iain Finley Davidson and Emanuel Kreidl and Georg Petzold and Jan-Michael Peters},
  booktitle={Current Biology},
  year={2014}
}
BACKGROUND Cohesin mediates sister chromatid cohesion by topologically entrapping sister DNA molecules inside its ring structure. Cohesin is loaded onto DNA by the Scc2/NIPBL-Scc4/MAU2-loading complex in a manner that depends on the adenosine triphosphatase (ATPase) activity of cohesin's Smc1 and Smc3 subunits. Subsequent cohesion establishment during DNA replication depends on Smc3 acetylation by Esco1 and Esco2 and on recruitment of sororin, which "locks" cohesin on DNA by inactivating the… CONTINUE READING
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