Cohesin Acetylation and ATPase Activity Control Cohesion and Loop Architecture through Distinct Mechanisms.

ABSTRACT: Cohesin is a conserved protein complex that mediates sister chromatid cohesion, chromosome condensation, gene regulation, and DNA repair. These processes rely on cohesin's ability to tether sister chromatids and form chromatin loops, which depend on cohesin's ATPase activity and Eco1-mediated acetylation of two lysine residues (K112 and K113 in budding yeast) in its Smc3 subunit. How cohesin's ATPase activity and acetylation integrate to control cohesin functions remains poorly understood. Here, we analyzed chromatin architecture in yeast mutants with altered cohesin acetylation and/or ATPase activity. We find that acetylation of either K112 or K113 is sufficient to produce a wild-type chromosome structure with loops positioned at cohesin-associated regions (CARs), whereas loss of acetylat

SUBMITTER: Costantino L 

PROVIDER: S-EPMC12636502 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature