Research Article

Structure of the RSC complex bound to the nucleosome

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Science  15 Nov 2019:
Vol. 366, Issue 6467, pp. 838-843
DOI: 10.1126/science.aay0033

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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

Abstract

The RSC complex remodels chromatin structure and regulates gene transcription. We used cryo–electron microscopy to determine the structure of yeast RSC bound to the nucleosome. RSC is delineated into the adenosine triphosphatase motor, the actin-related protein module, and the substrate recruitment module (SRM). RSC binds the nucleosome mainly through the motor, with the auxiliary subunit Sfh1 engaging the H2A-H2B acidic patch to enable nucleosome ejection. SRM is organized into three substrate-binding lobes poised to bind their respective nucleosomal epitopes. The relative orientations of the SRM and the motor on the nucleosome explain the directionality of DNA translocation and promoter nucleosome repositioning by RSC. Our findings shed light on RSC assembly and functionality, and they provide a framework to understand the mammalian homologs BAF/PBAF and the Sfh1 ortholog INI1/BAF47, which are frequently mutated in cancers.

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