ArticleThe Journal of biological chemistry2016
The Eaf3/5/7 Subcomplex Stimulates NuA4 Interaction with Methylated Histone H3 Lys-36 and RNA Polymerase II.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 19 citations in OpenAlex.
- Integrative approaches for predicting protein network perturbations through machine learning and structural characterization.Journal of proteomics · 2025Article
- Analysis of Whole-Genome for Identification of SevenInternational journal of molecular sciences · 2024Article
- Article
- Rice OsMRG702 and Its Partner OsMRGBP Control Flowering Time through H4 Acetylation.International journal of molecular sciences · 2023Article
- Biochemical Characterization of the TINTIN Module of the NuA4 Complex Reveals Allosteric Regulation of Nucleosome Interaction.Molecular and cellular biology · 2022Article
- A balancing act: interactions within NuA4/TIP60 regulate picNuA4 function in Saccharomyces cerevisiae and humans.Genetics · 2022Article
- Article
- Structural and functional specificity of H3K36 methylation.Epigenetics & chromatin · 2022Review
- Chromatin Regulators Ahc1p and Eaf3p Positively Influence Nitrogen Metabolism inFrontiers in microbiology · 2022Article
- New connections between ubiquitylation and methylation in the co-transcriptional histone modification network.Current genetics · 2021Review
- Transcription shapes genome-wide histone acetylation patterns.Nature communications · 2021Article
- Insights Into the Function of the NuA4 Complex in Plants.Frontiers in plant science · 2020Review
- ASH1-catalyzed H3K36 methylation drives gene repression and marks H3K27me2/3-competent chromatin.eLife · 2018Article
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
NuA4 is the only essential lysine acetyltransferase complex in Saccharomyces cerevisiae, where it has been shown to stimulate transcription initiation and elongation. Interaction with nucleosomes is stimulated by histone H3 Lys-4 and Lys-36 methylation, but the mechanism of this interaction is unknown. Eaf3, Eaf5, and Eaf7 form a subcomplex within NuA4 that may also function independently of the lysine acetyltransferase complex. The Eaf3/5/7 complex and the Rpd3C(S) histone deacetylase complex have both been shown to bind di- and trimethylated histone H3 Lys-36 stimulated by Eaf3. We investigated the role of the Eaf3/5/7 subcomplex in NuA4 binding to nucleosomes. Different phenotypes of eaf3/5/7Δ mutants support functions for the complex as both part of and independent of NuA4. Further evidence for Eaf3/5/7 within NuA4 came from mutations in the subcomplex leading to ∼40% reductions in H4 acetylation in bulk histones, probably caused by binding defects to both nucleosomes and RNA polymerase II. In vitro binding assays showed that Eaf3/5/7 specifically stimulates NuA4 binding to di- and trimethylated histone H3 Lys-36 and that this binding is important for NuA4 occupancy in transcribed ORFs. Consistent with the role of NuA4 in stimulating transcription elongation, loss of EAF5 or EAF7 resulted in a processivity defect. Overall, these results reveal the function of Eaf3/5/7 within NuA4 to be important for both NuA4 and RNA polymerase II binding.
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