ArticleMolecular and cellular biology2006
Deciphering the roles of the histone H2B N-terminal domain in genome-wide transcription.
Article in Molecular and cellular biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
55 citing papers in PubMed, 90 citations in OpenAlex.
- Downregulation of histone H2A and H2B pathways is associated with anthracycline sensitivity in breast cancer.Breast cancer research : BCR · 2016Trial
- Site-specific programming characterizes dynamic post-translational acetylation of histone H2B lysine 108 in mouse embryonic stem cells.Nature communications · 2026Article
- Unveiling the Conformational Dynamics of the Histone Tails Using Markov State Modeling.Journal of chemical theory and computation · 2025Article
- Conformational Dynamics of the Nucleosomal Histone H2B Tails Revealed by Molecular Dynamics Simulations.Journal of chemical information and modeling · 2024Article
- DNA Repair in Nucleosomes: Insights from Histone Modifications and Mutants.International journal of molecular sciences · 2024Review
- Characterization of a polyclonal antibody that is highly selective for the D-isoAsp-25 variant of mammalian histone H2B.Amino acids · 2023Article
- Local Alteration of Ionic Strength in a Nucleosome Core Particle and Its Effect onBiochemistry · 2022Article
- Trypanosoma brucei histones are heavily modified with combinatorial post-translational modifications and mark Pol II transcription start regions with hyperacetylated H2A.Nucleic acids research · 2022Article
- N-Terminal Tails of Histones H2A and H2B Differentially Affect Transcription by RNA Polymerase II In Vitro.Cells · 2022Article
- High-intensity interval training remodels the proteome and acetylome of human skeletal muscle.eLife · 2022Article
- Plant Histone HTB (H2B) Variants in Regulating Chromatin Structure and Function.Plants (Basel, Switzerland) · 2020Review
- Systematic genetic and proteomic screens during gametogenesis identify H2BK34 methylation as an evolutionary conserved meiotic mark.Epigenetics & chromatin · 2020Article
- TH2BS11ph histone mark is enriched in the unsynapsed axes of the XY body and predominantly associates with H3K4me3-containing genomic regions in mammalian spermatocytes.Epigenetics & chromatin · 2019Article
- Article
- Histone Tail Sequences Balance Their Role in Genetic Regulation and the Need To Protect DNA against Destruction in Nucleosome Core Particles Containing Abasic Sites.Chembiochem : a European journal of chemical biology · 2019Article
- Effects of histone H2B ubiquitylation on the nucleosome structure and dynamics.Nucleic acids research · 2018Article
- A cassette of basic amino acids in histone H2B regulates nucleosome dynamics and access to DNA damage.The Journal of biological chemistry · 2018Article
- Dissecting Nucleosome Function with a Comprehensive Histone H2A and H2B Mutant Library.G3 (Bethesda, Md.) · 2017Article
- The nucleoid as a scaffold for the assembly of bacterial signaling complexes.PLoS genetics · 2017Article
- Nucleosome Histone Tail Conformation and Dynamics: Impacts of Lysine Acetylation and a Nearby Minor Groove Benzo[a]pyrene-Derived Lesion.Biochemistry · 2017Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Histone N-terminal domains are frequent targets of posttranslational modifications. Multiple acetylated lysine residues have been identified in the N-terminal domain of H2B (K6, K11, K16, K17, K21, and K22), but little is known about how these modifications regulate transcription. We systematically mutated the N-terminal domain of histone H2B, both at known sites of lysine acetylation and elsewhere, and characterized the resulting changes in genome-wide expression in each mutant strain. Our results indicate that known sites of lysine acetylation in this domain are required for gene-specific transcriptional activation. However, the entire H2B N-terminal domain is principally required for the transcriptional repression of a large subset of the yeast genome. We find that the histone H2B repression (HBR) domain, comprised of residues 30 to 37, is necessary and sufficient for this repression. Many of the genes repressed by the HBR domain are located adjacent to telomeres or function in vitamin and carbohydrate metabolism. Deletion of the HBR domain also confers an increased sensitivity to DNA damage by UV irradiation. We mapped the critical residues in the HBR domain required for its repression function. Finally, comparisons of these data with previous studies reveal that a surprising number of genes are coregulated by the N-terminal domains of histone H2B, H3, and H4.
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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.