Journal
MOLECULAR CELL
Volume 79, Issue 6, Pages 917-+Publisher
CELL PRESS
DOI: 10.1016/j.molcel.2020.07.013
Keywords
-
Categories
Funding
- UK Medical Research Council [MC_PC_17136, FC001198, FC001065]
- European Research Council [670412, 820102]
- Francis Crick Institute
- Cancer Research UK [FC001198, FC001065]
- Wellcome Trust [FC001198, FC001065]
- Deutsche Forschungsgemeinschaft (DFG) [EXC 2008-390540038-UniSysCat]
- European Research Council (ERC) [670412, 820102] Funding Source: European Research Council (ERC)
- MRC [MC_PC_17136] Funding Source: UKRI
Ask authors/readers for more resources
Despite key roles in sister chromatid cohesion and chromosome organization, the mechanism by which cohesin rings are loaded onto DNA is still unknown. Here we combine biochemical approaches and cryoelectron microscopy (cryo-EM) to visualize a cohesin loading intermediate in which DNA is locked between two gates that lead into the cohesin ring. Building on this structural framework, we design experiments to establish the order of events during cohesin loading. In an initial step, DNA traverses an N-terminal kleisin gate that is first opened upon ATP binding and then closed as the cohesin loader locks the DNA against the ATPase gate. ATP hydrolysis will lead to ATPase gate opening to complete DNA entry. Whether DNA loading is successful or results in loop extrusion might be dictated by a conserved kleisin N-terminal tail that guides the DNA through the kleisin gate. Our results establish the molecular basis for cohesin loading onto DNA.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available