ArticlePLoS genetics2015
The Nucleosome Acidic Patch Regulates the H2B K123 Monoubiquitylation Cascade and Transcription Elongation in Saccharomyces cerevisiae.
Article in PLoS genetics, 2015. 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, 33 citations in OpenAlex.
- H2BE113K mutation promotes breast cancer metastasis through modulating chromatin dynamics.Science advances · 2026Article
- Trans-histone crosstalk establishes distinct H3K79 methylation zones with differential transcriptional functions.Nucleic acids research · 2026Article
- A direct interaction between the Chd1 CHCT domain and Rtf1 controls Chd1 distribution and nucleosome positioning on active genes.Nucleic acids research · 2025Article
- Histone H2B ubiquitylation: Connections to transcription and effects on chromatin structure.Biochimica et biophysica acta. Gene regulatory mechanisms · 2024Review
- The histone H2B Arg95 residue efficiently recruits the transcription factor Spt16 to mediate Ste5 expression of the pheromone response pathway.Scientific reports · 2023Article
- Spt6 directly interacts with Cdc73 and is required for Paf1 complex occupancy at active genes in Saccharomyces cerevisiae.Nucleic acids research · 2023Article
- Quantitative Assessment of Histone H2B Monoubiquitination in Yeast Using Immunoblotting.Methods and protocols · 2022Article
- Post-Translational Modifications of Histones Are Versatile Regulators of Fungal Development and Secondary Metabolism.Toxins · 2022Review
- The Paf1 Complex: A Keystone of Nuclear Regulation Operating at the Interface of Transcription and Chromatin.Journal of molecular biology · 2021Review
- Higher-order organization of biomolecular condensates.Open biology · 2021Review
- Specialized RSC: Substrate Specificities for a Conserved Chromatin Remodeler.BioEssays : news and reviews in molecular, cellular and developmental biology · 2020Article
- The histone H4 basic patch regulates SAGA-mediated H2B deubiquitination and histone acetylation.The Journal of biological chemistry · 2020Article
- The nucleosome acidic patch directly interacts with subunits of the Paf1 and FACT complexes and controls chromatin architecture in vivo.Nucleic acids research · 2019Article
- Residues in the Nucleosome Acidic Patch Regulate Histone Occupancy and Are Important for FACT Binding inGenetics · 2017Article
- The Histone Modification Domain of Paf1 Complex Subunit Rtf1 Directly Stimulates H2B Ubiquitylation through an Interaction with Rad6.Molecular cell · 2016Article
- Structural mechanism for the recognition and ubiquitination of a single nucleosome residue by Rad6-Bre1.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- The upstreams and downstreams of H3K79 methylation by DOT1L.Chromosoma · 2016Review
- Synthetic Nucleosomes Reveal that GlcNAcylation Modulates Direct Interaction with the FACT Complex.Angewandte Chemie (International ed. in English) · 2016Article
- Quantitative Analysis of Dynamic Protein Interactions during Transcription Reveals a Role for Casein Kinase II in Polymerase-associated Factor (PAF) Complex Phosphorylation and Regulation of Histone H2B Monoubiquitylation.The Journal of biological chemistry · 2016Article
- Recognition of the nucleosome by chromatin factors and enzymes.Current opinion in structural biology · 2016Review
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Eukaryotes regulate gene expression and other nuclear processes through the posttranslational modification of histones. In S. cerevisiae, the mono-ubiquitylation of histone H2B on lysine 123 (H2B K123ub) affects nucleosome stability, broadly influences gene expression and other DNA-templated processes, and is a prerequisite for additional conserved histone modifications that are associated with active transcription, namely the methylation of lysine residues in H3. While the enzymes that promote these chromatin marks are known, regions of the nucleosome required for the recruitment of these enzymes are undefined. To identify histone residues required for H2B K123ub, we exploited a functional interaction between the ubiquitin-protein ligase, Rkr1/Ltn1, and H2B K123ub in S. cerevisiae. Specifically, we performed a synthetic lethal screen with cells lacking RKR1 and a comprehensive library of H2A and H2B residue substitutions, and identified H2A residues that are required for H2B K123ub. Many of these residues map to the nucleosome acidic patch. The substitutions in the acidic patch confer varying histone modification defects downstream of H2B K123ub, indicating that this region contributes differentially to multiple histone modifications. Interestingly, substitutions in the acidic patch result in decreased recruitment of H2B K123ub machinery to active genes and defects in transcription elongation and termination. Together, our findings reveal a role for the nucleosome acidic patch in recruitment of histone modification machinery and maintenance of transcriptional integrity.
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