ArticleCell discovery2023
Two assembly modes for SIN3 histone deacetylase complexes.
Article in Cell discovery, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 15 citations in OpenAlex.
- Chromatin context-dependent deacetylation by the asymmetric Rpd3L.Nucleic acids research · 2026Article
- A sponge homolog of BRMS1 reveals ancient origin of metastasis-suppressing functions.BMC biology · 2026Article
- Article
- A de novo missense variant in MIDEAS results in increased deacetylase activity of the MiDAC HDAC complex causing a neurodevelopmental syndrome.Nature communications · 2025Article
- Mutations on the surface of HDAC1 reveal molecular determinants of specific complex assembly and their requirement for gene regulation.Nucleic acids research · 2025Article
- Inherent asymmetry of Rpd3S coordinates its nucleosome engagement and association with elongating RNA polymerase II.Nature structural & molecular biology · 2025Article
- Structures and dynamics of Rpd3S complex bound to nucleosome.Science advances · 2024Article
- Article
- Structure of the complete Saccharomyces cerevisiae Rpd3S-nucleosome complex.Nature communications · 2023Article
- Structural basis for nucleosome binding and catalysis by the yeast Rpd3S/HDAC holoenzyme.Cell research · 2023Article
- Structural basis of nucleosome deacetylation and DNA linker tightening by Rpd3S histone deacetylase complex.Cell research · 2023Article
- Whole-Genome Analyses Point to New Candidate Genes Underlying Estivation in Amphibians.Ecological and evolutionary physiologyReview
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.