Structure of SWI/SNF chromatin remodeller RSC bound to a nucleosome

Felix R. Wagner, Christian Dienemann, Haibo Wang, Alexandra Stützer, Dimitry Tegunov, Henning Urlaub and Patrick Cramer ()
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Felix R. Wagner: Department of Molecular Biology
Christian Dienemann: Department of Molecular Biology
Haibo Wang: Department of Molecular Biology
Alexandra Stützer: Bioanalytical Mass Spectrometry
Dimitry Tegunov: Department of Molecular Biology
Henning Urlaub: Bioanalytical Mass Spectrometry
Patrick Cramer: Department of Molecular Biology

Nature, 2020, vol. 579, issue 7799, 448-451

Abstract: Abstract Chromatin-remodelling complexes of the SWI/SNF family function in the formation of nucleosome-depleted, transcriptionally active promoter regions (NDRs)1,2. In the yeast Saccharomyces cerevisiae, the essential SWI/SNF complex RSC3 contains 16 subunits, including the ATP-dependent DNA translocase Sth14,5. RSC removes nucleosomes from promoter regions6,7 and positions the specialized +1 and −1 nucleosomes that flank NDRs8,9. Here we present the cryo-electron microscopy structure of RSC in complex with a nucleosome substrate. The structure reveals that RSC forms five protein modules and suggests key features of the remodelling mechanism. The body module serves as a scaffold for the four flexible modules that we call DNA-interacting, ATPase, arm and actin-related protein (ARP) modules. The DNA-interacting module binds extra-nucleosomal DNA and is involved in the recognition of promoter DNA elements8,10,11 that influence RSC functionality12. The ATPase and arm modules sandwich the nucleosome disc with the Snf2 ATP-coupling (SnAC) domain and the finger helix, respectively. The translocase motor of the ATPase module engages with the edge of the nucleosome at superhelical location +2. The mobile ARP module may modulate translocase–nucleosome interactions to regulate RSC activity5. The RSC–nucleosome structure provides a basis for understanding NDR formation and the structure and function of human SWI/SNF complexes that are frequently mutated in cancer13.

Date: 2020
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DOI: 10.1038/s41586-020-2088-0

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