8I03

Cryo-EM structure of the SIN3L complex from S. pombe

Summary for 8I03

• Entry DOI: 10.2210/pdb8i03/pdb
• EMDB information: 35093
• Descriptor: Paired amphipathic helix protein pst1, ZINC ION, POTASSIUM ION, ... (11 entities in total)
• Functional Keywords: sin3, sin3l, pst1, pst3, clr6, deacetylase, dna binding protein
• Biological source: Schizosaccharomyces pombe (fission yeast); More
• Total number of polymer chains: 11
• Total formula weight: 682715.02

Authors

Wang, C.,Guo, Z.,Zhan, X. (deposition date: 2023-01-10, release date: 2023-05-03, Last modification date: 2025-07-02)

Primary citation

Wang, C.,Guo, Z.,Chu, C.,Lu, Y.,Zhang, X.,Zhan, X.
Two assembly modes for SIN3 histone deacetylase complexes.
Cell Discov, 9:42-42, 2023

PubMed Abstract: The switch-independent 3 (SIN3)/histone deacetylase (HDAC) complexes play essential roles in regulating chromatin accessibility and gene expression. There are two major types of SIN3/HDAC complexes (named SIN3L and SIN3S) targeting different chromatin regions. Here we present the cryo-electron microscopy structures of the SIN3L and SIN3S complexes from Schizosaccharomyces pombe (S. pombe), revealing two distinct assembly modes. In the structure of SIN3L, each Sin3 isoform (Pst1 and Pst3) interacts with one histone deacetylase Clr6, and one WD40-containing protein Prw1, forming two lobes. These two lobes are bridged by two vertical coiled-coil domains from Sds3/Dep1 and Rxt2/Png2, respectively. In the structure of SIN3S, there is only one lobe organized by another Sin3 isoform Pst2; each of the Cph1 and Cph2 binds to an Eaf3 molecule, providing two modules for histone recognition and binding. Notably, the Pst1 Lobe in SIN3L and the Pst2 Lobe in SIN3S adopt similar conformation with their deacetylase active sites exposed to the space; however, the Pst3 Lobe in SIN3L is in a compact state with its active center buried inside and blocked. Our work reveals two classical organization mechanisms for the SIN3/HDAC complexes to achieve specific targeting and provides a framework for studying the histone deacetylase complexes.

PubMed: 37076472
DOI: 10.1038/s41421-023-00539-x

Experimental method

ELECTRON MICROSCOPY (3.2 Å)