ArticleMolecular cell2005
Histone H4 lysine 91 acetylation a core domain modification associated with chromatin assembly.
Article in Molecular cell, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 89 papers.
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Who cites it
89 citing papers in PubMed, 168 citations in OpenAlex.
- Site-specific programming characterizes dynamic post-translational acetylation of histone H2B lysine 108 in mouse embryonic stem cells.Nature communications · 2026Article
- Newly synthesized histones: passive or active players in the regulation of epigenetic inheritance?Nucleic acids research · 2026Review
- Epigenetic alterations in Myeloid Malignancies.Advances in experimental medicine and biology · 2026Review
- Characterization of endogenous SUMOylation sites by click chemistry-based proteomics.Analytical and bioanalytical chemistry · 2025Article
- Structural and thermodynamic impact of oncogenic mutations on the nucleosome core particle.Biophysical journal · 2025Article
- Crossing epigenetic frontiers: the intersection of novel histone modifications and diseases.Signal transduction and targeted therapy · 2024Review
- The Role of Sirtuin-1 Isoforms in Regulating Mitochondrial Function.Current issues in molecular biology · 2024Article
- The Role of Histone Modification in DNA Replication-Coupled Nucleosome Assembly and Cancer.International journal of molecular sciences · 2023Review
- NAA60 (HAT4): the newly discovered bi-functional Golgi member of the acetyltransferase family.Clinical epigenetics · 2022Review
- Downregulation of glob1 mitigates human tau mediated neurotoxicity by restricting heterochromatin loss and elevating the autophagic response in drosophila.Molecular biology reports · 2022Article
- Recurrent de novo missense variants across multiple histone H4 genes underlie a neurodevelopmental syndrome.American journal of human genetics · 2022Article
- Reprogramming of the epigenome in neurodevelopmental disorders.Critical reviews in biochemistry and molecular biology · 2022Review
- Acetylproteomics analyses reveal critical features of lysine-ε-acetylation in Arabidopsis and a role of 14-3-3 protein acetylation in alkaline response.Stress biology · 2022Article
- Roles of Negatively Charged Histone Lysine Acylations in Regulating Nucleosome Structure and Dynamics.Frontiers in molecular biosciences · 2022Review
- Mapping protein carboxymethylation sites provides insights into their role in proteostasis and cell proliferation.Nature communications · 2021Article
- Histone succinylation and its function on the nucleosome.Journal of cellular and molecular medicine · 2021Review
- Histone H2B Mutations in Cancer.Biomedicines · 2021Review
- The dark side of histones: genomic organization and role of oncohistones in cancer.Clinical epigenetics · 2021Review
- Semisynthesis of site-specifically succinylated histone reveals that succinylation regulates nucleosome unwrapping rate and DNA accessibility.Nucleic acids research · 2020Article
- Review
29 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
The acetylation of the NH2-terminal tail of histone H4 by type B histone acetyltransferases (HATs) is involved in the process of chromatin assembly. Histone H4 associated with a nuclear type B HAT complex contains modifications in its globular core domain as well. In particular, acetylation was found at lysine 91. A mutation that alters this residue, which lies in the interface between histone H3/H4 tetramers and H2A/H2B dimers, confers phenotypes consistent with defects in chromatin assembly such as sensitivity to DNA damaging agents and derepression and alteration of silent chromatin structure. In addition, this mutation destabilizes the histone octamer, leading to defects in chromatin structure. These results indicate an important role for histone modifications outside the NH2-tail domains in the processes of chromatin assembly, DNA repair, and transcriptional silencing.
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Registered trials
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