ArticleNucleic acids research2013
Replication-independent nucleosome exchange is enhanced by local and specific acetylation of histone H4.
Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Who cites it
10 citing papers in PubMed, 20 citations in OpenAlex.
- Usage of the H3 variants during the S-phase of the cell cycle in Physarum polycephalum.Nucleic acids research · 2022Article
- Replication-Coupled Chromatin Remodeling: An Overview of Disassembly and Assembly of Chromatin during Replication.International journal of molecular sciences · 2021Review
- Slowing Down Ageing: The Role of Nutrients and Microbiota in Modulation of the Epigenome.Nutrients · 2019Review
- Effect of oxidative stress from nanoscale TiOEnvironmental science and pollution research international · 2017Article
- Histones H3 and H4 require their relevant amino-tails for efficient nuclear import and replication-coupled chromatin assembly in vivo.Scientific reports · 2017Article
- Striatal H3K27 Acetylation Linked to Glutamatergic Gene Dysregulation in Human Heroin Abusers Holds Promise as Therapeutic Target.Biological psychiatry · 2017Article
- Hybrid phase ligation for efficient synthesis of histone proteins.Organic & biomolecular chemistry · 2016Article
- Review
- HIRA orchestrates a dynamic chromatin landscape in senescence and is required for suppression of neoplasia.Genes & development · 2014Article
- Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
We used a novel single-cell strategy to examine the fate of histones during G(2)-phase. Consistent with previous results, we find that in G(2)-phase, the majority of nuclear histones are assembled into chromatin, whereas a small fraction comprises an unassembled pool. Small increases in the amount of histones within the free pool affect the extent of exchange, suggesting that the free pool is in dynamic equilibrium with chromatin proteins. Unexpectedly, acetylated H4 is preferentially partitioned to the unassembled pool. Although an increase in global histone acetylation did not affect overall nucleosome dynamics, an H4 containing lysine to glutamine substitutions as mimics of acetylation significantly increased the rate of exchange, but did not affect the acetylation state of neighbouring nucleosomes. Interestingly, transcribed regions are particularly predisposed to exchange on incorporation of H4 acetylation mimics compared with surrounding regions. Our results support a model whereby histone acetylation on K8 and K16 specifically marks nucleosomes for eviction, with histones being rapidly deacetylated on reassembly.
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