ArticleThe Journal of biological chemistry2016
Site-specific Acetylation of Histone H3 Decreases Polymerase β Activity on Nucleosome Core Particles in Vitro.
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 24 papers.
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Who cites it
24 citing papers in PubMed, 31 citations in OpenAlex.
- Base excision repair in chromatin: A tug-of-war for DNA damage.DNA repair · 2025Review
- A Method for Constructing Nucleosome Arrays with Spatially Defined Histone PTMs and DNA Damage.Angewandte Chemie (International ed. in English) · 2025Article
- H3K14: A histone site closely related to diseases.Journal of Cancer · 2025Review
- Article
- DNA Repair in Nucleosomes: Insights from Histone Modifications and Mutants.International journal of molecular sciences · 2024Review
- Generation of Recombinant Nucleosomes Containing Site-Specific DNA Damage.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Structural basis for APE1 processing DNA damage in the nucleosome.Nature communications · 2022Article
- Preparation of Nucleosome Core Particles Complexed with DNA Repair Factors for Cryo-Electron Microscopy Structural Determination.Journal of visualized experiments : JoVE · 2022Article
- Obstacles and opportunities for base excision repair in chromatin.DNA repair · 2022Review
- Chaperoning histones at the DNA repair dance.DNA repair · 2021Review
- Molecular dynamics simulations reveal how H3K56 acetylation impacts nucleosome structure to promote DNA exposure for lesion sensing.DNA repair · 2021Article
- Symmetrical dimethylation of H4R3: A bridge linking DNA damage and repair upon oxidative stress.Redox biology · 2020Article
- Acetylation of the histone H3 tail domain regulates base excision repair on higher-order chromatin structures.Scientific reports · 2019Article
- Histone H3 Lysine 56 Acetylation Enhances AP Endonuclease 1-Mediated Repair of AP Sites in Nucleosome Core Particles.Biochemistry · 2019Article
- Organization of DNA damage, excision repair, and mutagenesis in chromatin: A genomic perspective.DNA repair · 2019Review
- Two factor authentication: Asf1 mediates crosstalk between H3 K14 and K56 acetylation.Nucleic acids research · 2019Article
- Oxidation of 8-Oxo-7,8-dihydro-2'-deoxyguanosine Leads to Substantial DNA-Histone Cross-Links within Nucleosome Core Particles.Chemical research in toxicology · 2018Article
- Initiating base excision repair in chromatin.DNA repair · 2018Review
- A cassette of basic amino acids in histone H2B regulates nucleosome dynamics and access to DNA damage.The Journal of biological chemistry · 2018Article
- Genome-wide maps of alkylation damage, repair, and mutagenesis in yeast reveal mechanisms of mutational heterogeneity.Genome research · 2017Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Histone posttranslational modifications have been associated with changes in chromatin structure necessary for transcription, replication, and DNA repair. Acetylation is one of the most studied and best characterized histone posttranslational modifications, but it is not known if histone acetylation modulates base excision repair of DNA lesions in chromatin. To address this question, we generated nucleosome core particles (NCPs) containing site-specifically acetylated H3K14 or H3K56 and measured repair of uracil and single-nucleotide gaps. We find that H3K56Ac and H3K14Ac do not significantly contribute to removal of uracils by uracil DNA glycosylase regardless of the translational or rotational position of the lesions within NCPs. In repair of single-nucleotide gaps, however, the presence of H3K56Ac or H3K14Ac in NCPs decreases the gap-filling activity of DNA polymerase β near the dyad center, with H3K14Ac exhibiting stronger inhibition. To a lesser extent, H3K56Ac induces a similar effect near the DNA ends. Moreover, using restriction enzyme accessibility, we detect no changes in NCP structure or dynamics between H3K14Ac-NCPs and WT-NCPs containing single-nucleotide gaps. Thus, acetylation at H3K56 and H3K14 in nucleosomes may promote alternative gap-filling pathways by inhibiting DNA polymerase β activity.
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Registered trials
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