ArticleNucleic acids research2016
A basic domain in the histone H2B N-terminal tail is important for nucleosome assembly by FACT.
Article in Nucleic acids research, 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, 25 citations in OpenAlex.
- 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
- Article
- N-Terminal Tails of Histones H2A and H2B Differentially Affect Transcription by RNA Polymerase II In Vitro.Cells · 2022Article
- Systematic genetic and proteomic screens during gametogenesis identify H2BK34 methylation as an evolutionary conserved meiotic mark.Epigenetics & chromatin · 2020Article
- Structural visualization of key steps in nucleosome reorganization by human FACT.Scientific reports · 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
- Charged residues on the side of the nucleosome contribute to normal Spt16-gene interactions in budding yeast.Epigenetics · 2018Article
- Dissecting Nucleosome Function with a Comprehensive Histone H2A and H2B Mutant Library.G3 (Bethesda, Md.) · 2017Article
- Residues in the Nucleosome Acidic Patch Regulate Histone Occupancy and Are Important for FACT Binding inGenetics · 2017Article
- Nucleosome Histone Tail Conformation and Dynamics: Impacts of Lysine Acetylation and a Nearby Minor Groove Benzo[a]pyrene-Derived Lesion.Biochemistry · 2017Article
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Authors and funding
9 authors at 1 institution in 1 country.
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Abstract
Nucleosome assembly in vivo requires assembly factors, such as histone chaperones, to bind to histones and mediate their deposition onto DNA. In yeast, the essential histone chaperone FACT (FAcilitates Chromatin Transcription) functions in nucleosome assembly and H2A-H2B deposition during transcription elongation and DNA replication. Recent studies have identified candidate histone residues that mediate FACT binding to histones, but it is not known which histone residues are important for FACT to deposit histones onto DNA during nucleosome assembly. In this study, we report that the histone H2B repression (HBR) domain within the H2B N-terminal tail is important for histone deposition by FACT. Deletion of the HBR domain causes significant defects in histone occupancy in the yeast genome, particularly at HBR-repressed genes, and a pronounced increase in H2A-H2B dimers that remain bound to FACT in vivo Moreover, the HBR domain is required for purified FACT to efficiently assemble recombinant nucleosomes in vitro We propose that the interaction between the highly basic HBR domain and DNA plays an important role in stabilizing the nascent nucleosome during the process of histone H2A-H2B deposition by FACT.
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