Cohesin is an ATPase that drives chromosome organization through the generation of intramolecular loops and sister chromatid cohesion. Cohesin's ATPase is stimulated by Scc2 binding but attenuated by acetylation of its Smc3 subunit. In this issue of Genes & Development, Boardman and colleagues (pp. 277-290) take a genetic approach to generate a mechanistic model for the opposing regulation of cohesin's ATPase by Scc2 and Smc3 acetylation. Their findings provide in vivo insight into how this important genome organizer functions in vivo.
Keywords: ATPase; ECO1; ESCO1; NIPBL; SCC2; SMC; acetylation; cohesin; cohesion.
© 2023 Massari and Marston; Published by Cold Spring Harbor Laboratory Press.