期刊
MOLECULAR CELL
卷 75, 期 2, 页码 224-+出版社
CELL PRESS
DOI: 10.1016/j.molcel.2019.05.023
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资金
- Cancer Research UK [12386, 26747]
- Wellcome Trust [107935/Z/15/Z]
- European Research Council [294401]
- European Research Council (ERC) [294401] Funding Source: European Research Council (ERC)
- Wellcome Trust [107935/Z/15/Z] Funding Source: Wellcome Trust
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.
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