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Mol Cell. 2019 Jul 25;75(2):224-237.e5. doi: 10.1016/j.molcel.2019.05.023. Epub 2019 Jun 11.

Sister DNA Entrapment between Juxtaposed Smc Heads and Kleisin of the Cohesin Complex.

Author information

1
Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
2
Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK. Electronic address: ashley.nasmyth@bioch.ox.ac.uk.

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

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