Structure of a SIN3-HDAC complex from budding yeast

SIN3-HDAC (histone deacetylases) complexes have important roles in facilitating local histone deacetylation to regulate chromatin accessibility and gene expression. Here, we present the cryo-EM structure of the budding yeast SIN3-HDAC complex Rpd3L at an average resolution of 2.6 angstrom. The structure reveals that two distinct arms (ARM1 and ARM2) hang on a T-shaped scaffold formed by two coiled-coil domains. In each arm, Sin3 interacts with different subunits to create a different environment for the histone deacetylase Rpd3. ARM1 is in the inhibited state with the active site of Rpd3 blocked, whereas ARM2 is in an open conformation with the active site of Rpd3 exposed to the exterior space. The observed asymmetric architecture of Rpd3L is different from those of available structures of other class I HDAC complexes. Our study reveals the organization mechanism of the SIN3-HDAC complex and provides insights into the interaction pattern by which it targets histone deacetylase to chromatin. Here, Zhouyan et al. present the structure of yeast SIN3-HDAC complex Rpd3L, revealing a distinctive organization mechanism compared with other class I HDAC complexes. The authors observe that two distinct arms hang on a T-shaped scaffold formed by two coiled-coil domains.

Automated summary

This study presents the cryo-EM structure of the yeast SIN3-HDAC complex Rpd3L, revealing a distinctive organization mechanism compared with other class I HDAC complexes. The structure shows two distinct arms that interact with different subunits, resulting in an asymmetric architecture of Rpd3L.