ArticleJournal of molecular biology2012
Sequence requirements for combinatorial recognition of histone H3 by the MRG15 and Pf1 subunits of the Rpd3S/Sin3S corepressor complex.
Article in Journal of molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 32 citations in OpenAlex.
- The C-terminal PHDVC5HCH tandem domain of NSD2 is a combinatorial reader of unmodified H3K4 and tri-methylated H3K27 that regulates transcription of cell adhesion genes in multiple myeloma.Nucleic acids research · 2025Article
- Structural and functional insights into the epigenetic regulator MRG15.Acta pharmacologica Sinica · 2024Review
- Structures and dynamics of Rpd3S complex bound to nucleosome.Science advances · 2024Article
- Article
- Structure of histone deacetylase complex Rpd3S bound to nucleosome.Nature structural & molecular biology · 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
- Article
- The Eaf3 chromodomain acts as a pH sensor for gene expression by altering its binding affinity for histone methylated-lysine residues.Bioscience reports · 2020Article
- Recognition of cancer mutations in histone H3K36 by epigenetic writers and readers.Epigenetics · 2018Review
- Shaping the cellular landscape with Set2/SETD2 methylation.Cellular and molecular life sciences : CMLS · 2017Review
- MRG15-mediated tethering of PALB2 to unperturbed chromatin protects active genes from genotoxic stress.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- The Chromatin-Associated Phf12 Protein Maintains Nucleolar Integrity and Prevents Premature Cellular Senescence.Molecular and cellular biology · 2017Article
- Combinatorial Histone Readout by the Dual Plant Homeodomain (PHD) Fingers of Rco1 Mediates Rpd3S Chromatin Recruitment and the Maintenance of Transcriptional Fidelity.The Journal of biological chemistry · 2016Article
- Structural Basis for Multi-specificity of MRG Domains.Structure (London, England : 1993) · 2015Article
- Histone exchange, chromatin structure and the regulation of transcription.Nature reviews. Molecular cell biology · 2015Review
- Nucleosome contact triggers conformational changes of Rpd3S driving high-affinity H3K36me nucleosome engagement.Cell reports · 2015Article
- Traceless semisynthesis of a set of histone 3 species bearing specific lysine methylation marks.Chembiochem : a European journal of chemical biology · 2014Article
- Alternative splicing of the chromodomain protein Morf4l1 pre-mRNA has implications on cell differentiation in the developing chicken retina.Journal of molecular neuroscience : MN · 2013Article
- A phylogenetic study of SPBP and RAI1: evolutionary conservation of chromatin binding modules.PloS one · 2013Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
The transcriptional output at a genomic locus in eukaryotes is determined, in part, by the pattern of histone modifications that are read and interpreted by key effector proteins. The histone deacetylase activity of the evolutionarily conserved Rpd3S/Sin3S complex is crucial for suppressing aberrant transcription from cryptic start sites within intragenic regions of actively transcribed genes. Precise targeting of the complex relies on the chromatin binding activities of the MRG15 (MRG stands for mortality factor on chromosome 4 related gene) and Pf1 subunits. Whereas the molecular target of the MRG15 chromodomain (CD) has been suggested to be H3K36me(2/3), the precise molecular target of the Pf1 plant homeodomain 1 (PHD1) has remained elusive. Here, we show that Pf1 PHD1 binds preferentially to the unmodified extreme N-terminus of histone H3 (H3K4me(0)) but not to H3K4me(2/3), which are enriched in the promoter and 5' regions of genes. Unlike previously characterized CD and PHD domains that bind to their targets with micromolar affinity, both MRG15 CD and Pf1 PHD1 bind to their targets with >100 μM affinity, offering an explanation for why both MRG15 CD and Pf1 PHD1 domains are required to target the Rpd3S/Sin3S complex to chromatin. Our results also suggest that bivalency, rather than cooperativity, is the operative mechanism by which Pf1 and MRG15 combine to engage H3 in a biologically significant manner. Finally, the studies reveal an unanticipated role of Pf1 PHD1 in engaging the MRG15 MRG domain, albeit in a Pf1 MRG-binding-domain-dependent manner, implying a key role for the MRG15 MRG-Pf1 MBD interaction in chromatin targeting of the Rpd3S/Sin3S complex.
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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.