The structural basis for cohesin–CTCF-anchored loops

Yan Li, Judith H. I. Haarhuis, Ángela Sedeño Cacciatore, Roel Oldenkamp, Marjon S. Ruiten, Laureen Willems, Hans Teunissen, Kyle W. Muir (), Elzo Wit (), Benjamin D. Rowland () and Daniel Panne ()
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Yan Li: European Molecular Biology Laboratory
Judith H. I. Haarhuis: The Netherlands Cancer Institute
Ángela Sedeño Cacciatore: The Netherlands Cancer Institute
Roel Oldenkamp: The Netherlands Cancer Institute
Marjon S. Ruiten: The Netherlands Cancer Institute
Laureen Willems: The Netherlands Cancer Institute
Hans Teunissen: The Netherlands Cancer Institute
Kyle W. Muir: European Molecular Biology Laboratory
Elzo Wit: The Netherlands Cancer Institute
Benjamin D. Rowland: The Netherlands Cancer Institute
Daniel Panne: European Molecular Biology Laboratory

Nature, 2020, vol. 578, issue 7795, 472-476

Abstract: Abstract Cohesin catalyses the folding of the genome into loops that are anchored by CTCF1. The molecular mechanism of how cohesin and CTCF structure the 3D genome has remained unclear. Here we show that a segment within the CTCF N terminus interacts with the SA2–SCC1 subunits of human cohesin. We report a crystal structure of SA2–SCC1 in complex with CTCF at a resolution of 2.7 Å, which reveals the molecular basis of the interaction. We demonstrate that this interaction is specifically required for CTCF-anchored loops and contributes to the positioning of cohesin at CTCF binding sites. A similar motif is present in a number of established and newly identified cohesin ligands, including the cohesin release factor WAPL2,3. Our data suggest that CTCF enables the formation of chromatin loops by protecting cohesin against loop release. These results provide fundamental insights into the molecular mechanism that enables the dynamic regulation of chromatin folding by cohesin and CTCF.

Date: 2020
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DOI: 10.1038/s41586-019-1910-z

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