ArticleThe Journal of biological chemistry2011
Structure of the 30-kDa Sin3-associated protein (SAP30) in complex with the mammalian Sin3A corepressor and its role in nucleic acid binding.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 40 citations in OpenAlex.
- Chromatin context-dependent deacetylation by the asymmetric Rpd3L.Nucleic acids research · 2026Article
- Multicomplex Integrative Structural Modeling of a Human Histone Deacetylase Interactome.bioRxiv : the preprint server for biology · 2026Article
- SAP30 deacetylates the Tas protein to inhibit PFV replication.Cell & bioscience · 2025Article
- SAP30, an oncogenic driver of progression, poor survival, and drug resistance in neuroblastoma.Molecular therapy. Nucleic acids · 2024Article
- Structure of histone deacetylase complex Rpd3S bound to nucleosome.Nature structural & molecular biology · 2023Article
- SAP30 promotes breast tumor progression by bridging the transcriptional corepressor SIN3 complex and MLL1.The Journal of clinical investigation · 2023Article
- Class I histone deacetylase complex: Structure and functional correlates.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Structure of a SIN3-HDAC complex from budding yeast.Nature structural & molecular biology · 2023Article
- Cryo-EM structure of the Saccharomyces cerevisiae Rpd3L histone deacetylase complex.Nature communications · 2023Article
- Mechanism of assembly, activation and lysine selection by the SIN3B histone deacetylase complex.Nature communications · 2023Article
- Two assembly modes for SIN3 histone deacetylase complexes.Cell discovery · 2023Article
- Targeting UHRF1-SAP30-MXD4 axis for leukemia initiating cell eradication in myeloid leukemia.Cell research · 2022Article
- Distinct biochemical properties of the class I histone deacetylase complexes.Current opinion in chemical biology · 2022Review
- Establishment of Novel Protein Interaction Assays between Sin3 and REST Using Surface Plasmon Resonance and Time-Resolved Fluorescence Energy Transfer.International journal of molecular sciences · 2021Article
- Connecting the αα-hubs: same fold, disordered ligands, new functions.Cell communication and signaling : CCS · 2021Article
- Expression of the Neural REST/NRSF-SIN3 Transcriptional Corepressor Complex as a Target for Small-Molecule Inhibitors.Molecular biotechnology · 2021Article
- Molecular specializations of deep cortical layer analogs in songbirds.Scientific reports · 2020Article
- The neuronal transcription factor Myt1L interacts via a conserved motif with the PAH1 domain of Sin3 to recruit the Sin3L/Rpd3L histone deacetylase complex.FEBS letters · 2020Article
- Integrative Modeling of a Sin3/HDAC Complex Sub-structure.Cell reports · 2020Article
- Inositol phosphates and core subunits of the Sin3L/Rpd3L histone deacetylase (HDAC) complex up-regulate deacetylase activity.The Journal of biological chemistry · 2019Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
The ∼2-megadalton evolutionarily conserved histone deacetylase-associated Rpd3L/Sin3L complex plays critical roles in altering the histone code and repressing transcription of a broad range of genes involved in many aspects of cellular physiology. Targeting of this complex to specific regions of the genome is presumed to rely on interactions involving one or more of at least 10 distinct subunits in the complex. Here we describe the solution structure of the complex formed by the interacting domains of two constitutively associated subunits, mSin3A and SAP30. The mSin3A paired amphipathic helix 3 (PAH3) domain in the complex adopts the left-handed four-helix bundle structure characteristic of PAH domains. The SAP30 Sin3 interaction domain (SID) binds to PAH3 via a tripartite structural motif, including a C-terminal helix that targets the canonical PAH hydrophobic cleft while two other helices and an N-terminal extension target a discrete surface formed largely by the PAH3 α2, α3, and α3' helices. The protein-protein interface is extensive (∼1400 Å(2)), accounting for the high affinity of the interaction and the constitutive association of the SAP30 subunit with the Rpd3L/Sin3L complex. We further show using NMR that the mSin3A PAH3-SAP30 SID complex can bind to nucleic acids, hinting at a role for a nucleolar localization sequence in the SID αA helix in targeting the Rpd3L/Sin3L complex for silencing ribosomal RNA genes.
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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 OpenQuestion graph.