Abstract
SWI/SNF remodelers play a key role in regulating chromatin architecture and gene expression. Here, we report the cryo-EM structure of the Saccharomyces cerevisiae Swi/Snf complex in a nucleosome-free state. The structure consists of a stable triangular base module and a flexible Arp module. The conserved subunits Swi1 and Swi3 form the backbone of the complex and closely interact with other components. Snf6, which is specific for yeast Swi/Snf complex, stabilizes the binding of the ATPase-containing subunit Snf2 to the base module. Comparison of the yeast Swi/Snf and RSC complexes reveals conserved structural features that govern the assembly and function of these two subfamilies of chromatin remodelers. Our findings complement those from recent structures of the yeast and human chromatin remodelers and provide further insights into the assembly and function of the SWI/SNF remodelers.
Highlights
SWI/SNF remodelers play a key role in regulating chromatin architecture and gene expression
The intact 12-subunits Swi/Snf complex was endogenously purified from S. cerevisiae by employing a C-terminal Flag tag on Snf[6] (Supplementary Fig. 1)
The overall structure can be divided into five main lobes, corresponding to the rigid core, the nucleosome binding (NB) module, the preHSA stabilization (PS) module, the coiled coil (CC) domain, and the Arp module, respectively (Fig. 1b)
Summary
SWI/SNF remodelers play a key role in regulating chromatin architecture and gene expression. Comparison of the yeast Swi/Snf and RSC complexes reveals conserved structural features that govern the assembly and function of these two subfamilies of chromatin remodelers. 1234567890():,; SWI/SNF remodelers, which are highly conserved from yeast to humans, alter histone−DNA interactions and play critical roles in the regulation of chromatin architecture and gene expression. The Saccharomyces cerevisiae Swi/Snf complex, which was the first chromatin remodeler discovered, consists of 12 proteins with a combined molecular weight of ~1 megadaltons (MDa)[5,6,7]. The components of the S. cerevisiae Swi/Snf complex were identified in the 1990s10–14, how these subunits contribute to the stability and function of the complex is poorly understood. The overall structure is similar to that of other SWI/SNF complexes, it still reveals a set of striking features that advance mechanistic understanding of complex organization
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