ArticleThe Journal of biological chemistry2010
A nucleosome surface formed by histone H4, H2A, and H3 residues is needed for proper histone H3 Lys36 methylation, histone acetylation, and repression of cryptic transcription.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 42 citations in OpenAlex.
- Regulation of the histone H3K36 methyltransferase Set2 by the histone chaperone Spt6.Nucleic acids research · 2026Article
- Regulation of the histone H3K36 methyltransferase Set2 by the histone chaperone Spt6.bioRxiv : the preprint server for biology · 2026Article
- Multiomic screening platform uncovers the impact of histone mutations on chromatin and cell fate.bioRxiv : the preprint server for biology · 2026Article
- Structural basis of H3K36 trimethylation by SETD2 during chromatin transcription.Science (New York, N.Y.) · 2025Article
- Spt5 orchestrates cryptic transcript suppression and transcriptional directionality.Communications biology · 2024Article
- Structural and functional specificity of H3K36 methylation.Epigenetics & chromatin · 2022Review
- Ready, SET, Go: Post-translational regulation of the histone lysine methylation network in budding yeast.The Journal of biological chemistry · 2021Review
- Surprising phenotypic diversity of cancer-associated mutations of Gly 34 in the histone H3 tail.eLife · 2021Article
- Genetic interaction mapping informs integrative structure determination of protein complexes.Science (New York, N.Y.) · 2020Article
- The conserved elongation factor Spn1 is required for normal transcription, histone modifications, and splicing in Saccharomyces cerevisiae.Nucleic acids research · 2020Article
- Article
- Unique and Shared Roles for Histone H3K36 Methylation States in Transcription Regulation Functions.Cell reports · 2020Article
- Regulation of alternative polyadenylation in the yeast Saccharomyces cerevisiae by histone H3K4 and H3K36 methyltransferases.Nucleic acids research · 2020Article
- Nucleosome and ubiquitin position Set2 to methylate H3K36.Nature communications · 2019Article
- A conserved genetic interaction between Spt6 and Set2 regulates H3K36 methylation.Nucleic acids research · 2019Article
- Bidirectional terminators: an underestimated aspect of gene regulation.Current genetics · 2018Review
- Shaping the cellular landscape with Set2/SETD2 methylation.Cellular and molecular life sciences : CMLS · 2017Review
- Article
- Bidirectional terminators in Saccharomyces cerevisiae prevent cryptic transcription from invading neighboring genes.Nucleic acids research · 2017Article
- Balancing acts of SRI and an auto-inhibitory domain specify Set2 function at transcribed chromatin.Nucleic acids research · 2015Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Set2-mediated H3 Lys(36) methylation is a histone modification that has been demonstrated to function in transcriptional elongation by recruiting the Rpd3S histone deacetylase complex to repress intragenic cryptic transcription. Recently, we identified a trans-histone pathway in which the interaction between the N terminus of Set2 and histone H4 Lys(44) is needed to mediate trans-histone H3 Lys(36) di- and trimethylation. In the current study, we demonstrate that mutation of the lysine 44 residue in histone H4 or the Set2 mutant lacking the histone H4 interaction motif leads to intragenic cryptic transcripts, indicating that the Set2 and histone H4 interaction is important to repress intragenic cryptic transcription. We also determine that histone H2A residues (Leu(116) and Leu(117)), which are in close proximity to histone H4 Lys(44), are needed for proper trans-histone H3 Lys(36) methylation. Similar to H4 Lys(44) mutants, histone H2A Leu(116) and Leu(117) mutations exhibited decreased H3 Lys(36) di- and trimethylation, increased histone H4 acetylation, increased resistance to 6-azauracil, and cryptic transcription. Interestingly, the combined histone H4 Lys(44) and H2A mutations have more severe methylation defects and increased H4 acetylation levels. Furthermore, we identify that additional histone H2A and H3 core residues are also needed for H3 Lys(36) di- and trimethylation. Overall, our results show and suggest that multiple H4, H2A, and H3 residues contribute to and form a Set2 docking/recognition site on the nucleosomal surface so that proper Set2-mediated H3 Lys(36) di- and trimethylation, histone acetylation, and transcriptional elongation can occur.
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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.