Cryo-EM structure of the human cohesin-NIPBL-DNA complex

Author:

Shi Zhubing1ORCID,Gao Haishan1ORCID,Bai Xiao-chen23ORCID,Yu Hongtao14ORCID

Affiliation:

1. Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.

2. Department of Biophysics, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.

3. Department of Cell Biology, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.

4. School of Life Sciences, Westlake University, Hangzhou, Zhejiang 310024, China.

Abstract

A blueprint to understand cohesin Cohesin is a multiprotein complex that entraps sister chromatids for chromosome segregation and regulates transcription by extruding DNA loops to shape DNA organization. Shi et al. determined the structure of human cohesin bound to the protein NIBPL, which helps load cohesin onto DNA, and DNA at medium resolution by cryo–electron microscopy. Two adenosine triphosphatase domains play a key role in cohesin function. The structure explains how NIBPL and DNA synergistically activate these domains and gives insight into how DNA is trapped by cohesin. Science , this issue p. 1454

Funder

Welch Foundation

Cancer Prevention and Research Institute of Texas

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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