Cohesin Releases DNA through Asymmetric ATPase-Driven Ring Opening

AMO Elbatsh, JHI Haarhuis, N Petela, C Chapard, A Fish, PH Celie, M Stadnik, D. Ristic, C.L. Wyman, RH Medema, K Nasmyth, BD Rowland

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Cohesin stably holds together the sister chromatids from S phase until mitosis. To do so, cohesin must be protected against its cellular antagonist Wapl. Eco1 acetylates cohesin's Smc3 subunit, which locks together the sister DNAs. We used yeast genetics to dissect how Wapl drives cohesin from chromatin and identified mutants of cohesin that are impaired in ATPase activity but remarkably confer robust cohesion that bypasses the need for the cohesin protectors Eco1 in yeast and Sororin in human cells. We uncover a functional asymmetry within the heart of cohesin's highly conserved ABC-like ATPase machinery and find that both ATPase sites contribute to DNA loading, whereas DNA release is controlled specifically by one site. We propose that Smc3 acetylation locks cohesin rings around the sister chromatids by counteracting an activity associated with one of cohesin's two ATPase sites.
Original languageUndefined/Unknown
Pages (from-to)575-588
Number of pages14
JournalMolecular Cell
Issue number4
Publication statusPublished - 2016

Research programs

  • EMC MGC-01-12-03
  • EMC MM-03-32-04

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