Structure of the RSC complex bound to the nucleosome

Author:

Ye Youpi12ORCID,Wu Hao23ORCID,Chen Kangjing12ORCID,Clapier Cedric R.4,Verma Naveen4ORCID,Zhang Wenhao2ORCID,Deng Haiteng2ORCID,Cairns Bradley R.4,Gao Ning5,Chen Zhucheng126ORCID

Affiliation:

1. MOE Key Laboratory of Protein Science, Tsinghua University, Beijing 100084, P.R. China.

2. School of Life Science, Tsinghua University, Beijing 100084, P.R. China.

3. Peking University–Tsinghua University–National Institute of Biological Sciences Joint Graduate Program, Beijing 100084, China.

4. Howard Hughes Medical Institute and Department of Oncological Sciences, Huntsman Cancer Institute, University of Utah School of Medicine, Salt Lake City, UT 84112, USA.

5. State Key Laboratory of Membrane Biology, Peking-Tsinghua Joint Center for Life Sciences, School of Life Sciences, Peking University, Beijing 100871, China.

6. Tsinghua-Peking Joint Center for Life Sciences, Beijing Advanced Innovation Center for Structural Biology, Beijing 100084, China.

Abstract

The architecture of the RSC complex RSC is a Snf2-family chromatin remodeler complex that controls the promoter architecture of most of the genes in yeast. Using single-particle cryo–electron microscopy, Ye et al. determined the structure of RSC bound to the nucleosome. The structure reveals the modular architecture of RSC, shows how RSC engages the nucleosome, and explains the remodeling directionality. RSC shows strong similarities to homologous human complexes that are frequently mutated in cancers, and this structure provides valuable information for understanding these systems. Science , this issue p. 838

Funder

National Natural Science Foundation of China

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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