Cryo-EM structure of SWI/SNF complex bound to a nucleosome.

ABSTRACT: The chromatin-remodelling complex SWI/SNF is highly conserved and has critical roles in various cellular processes, including transcription and DNA-damage repair^1,2. It hydrolyses ATP to remodel chromatin structure by sliding and evicting histone octamers^3-8, creating DNA regions that become accessible to other essential factors. However, our mechanistic understanding of the remodelling activity is hindered by the lack of a high-resolution structure of complexes from this family. Here we report the cryo-electron microscopy structure of Saccharomyces cerevisiae SWI/SNF bound to a nucleosome, at near-atomic resolution. In the structure, the actin-related protein (Arp) module is sandwiched between the ATPase and the rest of the complex, with the Snf2 helicase-SANT associ

SUBMITTER: Han Y 

PROVIDER: S-EPMC7319049 | biostudies-literature | 2020 Mar

REPOSITORIES: biostudies-literature