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Title: Cohesin releases DNA through asymmetric ATPase-driven ring opening      
keywords:
Epigenomics
ID:
PRJNA308861
description:
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 an unexpected functional asymmetry within the heart of cohesin’s highly conserved ABC-like ATPase machinery and show that an activity associated with one of cohesin’s two ATPase sites drives DNA release from cohesin rings. This key mechanism is conserved from yeast to humans. We propose that Eco1 locks cohesin rings around the sister chromatids by counteracting an asymmetric cohesin-associated ATPase activity. Overall design: Effect of mutations in Smc1 and Smc3 on cohesin loading onto chromosomes
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landingpage: http://www.ncbi.nlm.nih.gov/bioproject/PRJNA308861
authentication:
none
authorization:
none
ID:
pmid:26895426
name:
Saccharomyces cerevisiae
ncbiID:
ncbitax:4932
abbreviation:
NCBI
homePage: http://www.ncbi.nlm.nih.gov
ID:
SCR:006472
name:
National Center for Biotechnology Information
homePage: http://www.ncbi.nlm.nih.gov/bioproject
ID:
SCR:004801
name:
NCBI BioProject