粘蛋白
CTCF公司
染色质
遗传学
细胞生物学
生物
计算生物学
化学
DNA
基因
转录因子
增强子
作者
Yan Li,Judith H.I. Haarhuis,Ángela Sedeño Cacciatore,Roel Oldenkamp,Marjon S. van Ruiten,Laureen Willems,Hans Teunissen,Kyle Muir,Elzo de Wit,Benjamin D. Rowland,Daniel Panne
出处
期刊:Nature
[Springer Nature]
日期:2020-01-06
卷期号:578 (7795): 472-476
被引量:255
标识
DOI:10.1038/s41586-019-1910-z
摘要
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.
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