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The structural basis for cohesin-CTCF-anchored loops

Nature (London), 2020-02, Vol.578 (7795), p.472-476 [Peer Reviewed Journal]

COPYRIGHT 2020 Nature Publishing Group ;COPYRIGHT 2020 Nature Publishing Group ;Copyright Nature Publishing Group Feb 20, 2020 ;ISSN: 0028-0836 ;EISSN: 1476-4687 ;DOI: 10.1038/s41586-019-1910-z ;PMID: 31905366

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Title:
The structural basis for cohesin-CTCF-anchored loops
Author: Li, Yan ; Haarhuis, Judith H I ; Sedeño Cacciatore, Ángela ; Oldenkamp, Roel ; van Ruiten, Marjon S ; Willems, Laureen ; Teunissen, Hans ; Muir, Kyle W ; de Wit, Elzo ; Rowland, Benjamin D ; Panne, Daniel
Subjects: Amino acids ; Analysis ; bHLH proteins ; Binding Sites ; Carrier Proteins - metabolism ; CCCTC-Binding Factor - chemistry ; CCCTC-Binding Factor - metabolism ; Cell Cycle Proteins - chemistry ; Cell Cycle Proteins - metabolism ; Chromatin ; Chromatin - chemistry ; Chromatin - metabolism ; Chromosomal Proteins, Non-Histone - chemistry ; Chromosomal Proteins, Non-Histone - metabolism ; Cohesin ; Cohesins ; Cohesion ; Competition ; Control ; Crystal structure ; Crystallography, X-Ray ; DNA - chemistry ; DNA - metabolism ; Folding ; Genomes ; Humans ; Ligands ; Models, Molecular ; Mutation ; Nuclear Proteins - metabolism ; Peptide Fragments - chemistry ; Peptide Fragments - metabolism ; Peptides ; Protein Binding ; Protein Stability ; Protein Subunits - chemistry ; Protein Subunits - metabolism ; Proto-Oncogene Proteins - metabolism ; Structure ; Zinc finger proteins
Is Part Of: Nature (London), 2020-02, Vol.578 (7795), p.472-476
Description: Cohesin catalyses the folding of the genome into loops that are anchored by CTCF . 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 WAPL . 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.
Publisher: England: Nature Publishing Group
Language: English
Identifier: ISSN: 0028-0836
EISSN: 1476-4687
DOI: 10.1038/s41586-019-1910-z
PMID: 31905366
Source: ProQuest One Psychology
MEDLINE
ProQuest Central

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The structural basis for cohesin-CTCF-anchored loops

COPYRIGHT 2020 Nature Publishing Group ;COPYRIGHT 2020 Nature Publishing Group ;Copyright Nature Publishing Group Feb 20, 2020 ;ISSN: 0028-0836 ;EISSN: 1476-4687 ;DOI: 10.1038/s41586-019-1910-z ;PMID: 31905366

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