ArticleJournal of molecular biology2011
Solution structure of the mSin3A PAH2-Pf1 SID1 complex: a Mad1/Mxd1-like interaction disrupted by MRG15 in the Rpd3S/Sin3S complex.
Article in Journal of molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 34 citations in OpenAlex.
- Stability and interaction defects in the Sin3A-PAH1 αα-hub domain associated with loss-of-function variants.The Journal of biological chemistry · 2026Article
- Structural and functional insights into the epigenetic regulator MRG15.Acta pharmacologica Sinica · 2024Review
- Article
- Class I histone deacetylase complex: Structure and functional correlates.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Functional characterization and comparative analysis of gene repression-mediating domains interacting with yeast pleiotropic corepressors Sin3, Cyc8 and Tup1.Current genetics · 2023Article
- Article
- Article
- Structural Insight into the Binding of TGIF1 to SIN3A PAH2 Domain through a C-Terminal Amphipathic Helix.International journal of molecular sciences · 2021Article
- 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
- Co-repressor, co-activator and general transcription factor: the many faces of the Sin3 histone deacetylase (HDAC) complex.The Biochemical journal · 2018Review
- Mortality factor 4 like 1 protein mediates epithelial cell death in a mouse model of pneumonia.Science translational medicine · 2015Article
- Article
- Molecular Basis for the Mechanism of Constitutive CBP/p300 Coactivator Recruitment by CRTC1-MAML2 and Its Implications in cAMP Signaling.Biochemistry · 2015Article
- Structural Basis for Multi-specificity of MRG Domains.Structure (London, England : 1993) · 2015Article
- Histone deacetylase 2 (HDAC2) protein-dependent deacetylation of mortality factor 4-like 1 (MORF4L1) protein enhances its homodimerization.The Journal of biological chemistry · 2014Article
- Phosphoproteomics screen reveals akt isoform-specific signals linking RNA processing to lung cancer.Molecular cell · 2014Article
- Characterization of native protein complexes and protein isoform variation using size-fractionation-based quantitative proteomics.Molecular & cellular proteomics : MCP · 2013Article
- Sequence requirements for combinatorial recognition of histone H3 by the MRG15 and Pf1 subunits of the Rpd3S/Sin3S corepressor complex.Journal of molecular biology · 2012Article
- Sin3 interacts with Foxk1 and regulates myogenic progenitors.Molecular and cellular biochemistry · 2012Article
- Structural basis for molecular interactions involving MRG domains: implications in chromatin biology.Structure (London, England : 1993) · 2012Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Histone deacetylation constitutes an important mechanism for silencing genes. The histone-deacetylase-associated mammalian Rpd3S/Sin3S corepressor complex plays key roles in repressing aberrant gene transcription from cryptic transcription initiation sites and in mitigating RNA polymerase II progression in intragenic regions of actively transcribed genes. The Sin3 corepressor functions as a molecular adaptor linking histone deacetylases on the one hand, with the chromatin targeting subunits Pf1 and MRG15 on the other. Pf1 also functions as an adaptor by interacting with MRG15 and engaging in multivalent interactions with Sin3 targeting among other domains the two N-terminal paired amphipathic helix (PAH) domains that serve as sites of interaction with sequence-specific DNA-binding transcription factors. Here, we structurally and functionally evaluate the interaction between the PAH2 domain of mSin3A and the Sin3 interaction domain 1 (SID1) motif of Pf1 and find the structural aspects to be reminiscent of the interaction between the Mad1/Mxd1 transcription factor and Sin3. Pf1 residues within a highly conserved sequence motif immediately C-terminal to SID1 appear not to be important for the interaction with Sin3 PAH2. Unexpectedly, the MRG15 subunit competes, rather than collaborates, with Sin3 for the Pf1 segment encompassing the two conserved motifs, implying competition between two subunits for another subunit of the same chromatin-modifying complex.
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Registered trials
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