ArticleMolecular and cellular biology2013
Sites of acetylation on newly synthesized histone H4 are required for chromatin assembly and DNA damage response signaling.
Article in Molecular and cellular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 34 citations in OpenAlex.
- Newly synthesized histones: passive or active players in the regulation of epigenetic inheritance?Nucleic acids research · 2026Review
- Stabilization of the MAPK-Epigenetic Signaling Axis Underlies the Protective Effect of Thyme Oil Against Cadmium Stress in Root Meristem Cells ofInternational journal of molecular sciences · 2025Article
- Review
- The Role of Histone Modification in DNA Replication-Coupled Nucleosome Assembly and Cancer.International journal of molecular sciences · 2023Review
- The Role of PARP1 and PAR in ATP-Independent Nucleosome Reorganisation during the DNA Damage Response.Genes · 2022Review
- Post-Translational Modifications by Lipid Metabolites during the DNA Damage Response and Their Role in Cancer.Biomolecules · 2022Review
- Histone variants: The unsung guardians of the genome.DNA repair · 2022Review
- The asymmetric distribution of RNA polymerase II and nucleosomes on replicated daughter genomes is caused by differences in replication timing between the lagging and the leading strand.Genome research · 2022Article
- Article
- Histone acetyltransferase 1 is required for DNA replication fork function and stability.The Journal of biological chemistry · 2020Article
- Fluctuations of Histone Chemical Modifications in Breast, Prostate, and Colorectal Cancer: An Implication of Phytochemicals as Defenders of Chromatin Equilibrium.Biomolecules · 2019Review
- Hat1 acetylates histone H4 and modulates the transcriptional program in Drosophila embryogenesis.Scientific reports · 2019Article
- Early-onset aging and mitochondrial defects associated with loss of histone acetyltransferase 1 (Hat1).Aging cell · 2019Article
- Detection and Quantitation of Acetylated Histones on Replicating DNA Using In Situ Proximity Ligation Assay and Click-It Chemistry.Methods in molecular biology (Clifton, N.J.) · 2019Article
- Mechanistic insights into histone deposition and nucleosome assembly by the chromatin assembly factor-1.Nucleic acids research · 2018Review
- Rpb9-deficient cells are defective in DNA damage response and require histone H3 acetylation for survival.Scientific reports · 2018Article
- PP32 and SET/TAF-Iβ proteins regulate the acetylation of newly synthesized histone H4.Nucleic acids research · 2017Article
- Identification of multiple roles for histone acetyltransferase 1 in replication-coupled chromatin assembly.Nucleic acids research · 2017Article
- Review
- Histone hypoacetylation-activated genes are repressed by acetyl-CoA- and chromatin-mediated mechanism.Biochimica et biophysica acta · 2014Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
The best-characterized acetylation of newly synthesized histone H4 is the diacetylation of the NH2-terminal tail on lysines 5 and 12. Despite its evolutionary conservation, this pattern of modification has not been shown to be essential for either viability or chromatin assembly in any model organism. We demonstrate that mutations in histone H4 lysines 5 and 12 in yeast confer hypersensitivity to replication stress and DNA-damaging agents when combined with mutations in histone H4 lysine 91, which has also been found to be a site of acetylation on soluble histone H4. In addition, these mutations confer a dramatic decrease in cell viability when combined with mutations in histone H3 lysine 56. We also show that mutation of the sites of acetylation on newly synthesized histone H4 results in defects in the reassembly of chromatin structure that accompanies the repair of HO-mediated double-strand breaks. This defect is not due to a decrease in the level of histone H3 lysine 56 acetylation. Intriguingly, mutations that alter the sites of newly synthesized histone H4 acetylation display a marked decrease in levels of phosphorylated H2A (γ-H2AX) in chromatin surrounding the double-strand break. These results indicate that the sites of acetylation on newly synthesized histones H3 and H4 can function in nonoverlapping ways that are required for chromatin assembly, viability, and DNA damage response signaling.
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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.