美国德克萨斯大学西南医学中心Hongtao Yu、Xiao-chen Bai等研究人员，合作解析了人源cohesin-NIPBL-DNA复合物的冷冻电镜结构。2020年5月15日，《科学》杂志在线发表了这一最新研究成果。
Title: Cryo-EM structure of the human cohesin-NIPBL-DNA complex
Author: Zhubing Shi, Haishan Gao, Xiao-chen Bai, Hongtao Yu
Abstract: Abstract As a ring-shaped ATPase machine, cohesin organizes the eukaryotic genome by extruding DNA loops and mediates sister-chromatid cohesion by topologically entrapping DNA. How cohesin executes these fundamental DNA transactions is not understood. Using cryo-electron microscopy, we determine the structure of human cohesin bound to its loader NIPBL and DNA at medium resolution. Cohesin and NIPBL interact extensively and together form a central tunnel to entrap a 72-base pair DNA. NIPBL and DNA promote the engagement of cohesin’s ATPase head domains and ATP binding. The hinge domains of cohesin adopt an “open washer” conformation and dock onto the STAG1 subunit. Our structure explains the synergistic activation of cohesin by NIPBL and DNA, and provides insight into DNA entrapment by cohesin.