Abstract
Cohesin entraps sister DNAs within tripartite rings created by pairwise interactions between Smc1, Smc3, and Scc1. Because Smc1/3 ATPase heads can also interact with each other, cohesin rings have the potential to form a variety of sub-compartments. Using in vivo cysteine cross-linking, we show that when Smc1 and Smc3 ATPases are engaged in the presence of ATP (E heads), cohesin rings generate a "SMC (S) compartment" between hinge and E heads and a "kleisin (K) compartment" between E heads and their associated kleisin subunit. Upon ATP hydrolysis, cohesin's heads associate in a different mode, in which their signature motifs and their coiled coils are closely juxtaposed (J heads), creating alternative S and K compartments. We show that K compartments of either E or J type can entrap single DNAs, that acetylation of Smc3 during S phase is associated with J heads, and that sister DNAs are entrapped in J-K compartments.
Keywords:
DNA; S and K compartments; Scc1; Smc ATPase domains; acetylation; cohesin rings; engaged; entrapment; juxtaposed.