Regulation of chromatin by histone modifications
Open accessAbstract
Chromatin is not an inert structure, but rather an instructive DNA scaffold that can respond to external cues to regulate the many uses of DNA. A principle component of chromatin that plays a key role in this regulation is the modification of histones. There is an ever-growing list of these modifications and the complexity of their action is only just beginning to be understood. However, it is clear that histone modifications play fundamental roles in most biological processes that are involved in the manipulation and expression of DNA. Here, we describe the known histone modifications, define where they are found genomically and discuss some of their functional consequences, concentrating mostly on transcription where the majority of characterisation has taken place.
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The acetylation state of histones is regulated by histone acetyltransferases, which add acetyl groups to histone tails at lysine residues, and histone deacetylases, which remove these acetyl groups.
“The acetylation state of histones is regulated by the following two classes of enzymes: histone acetyltransferases (HATs), which add acetyl groups to histone tails at lysine residues, and histone deacetylases (HDACs), which removes these acetyl groups.”
From The Epigenetics of Anxiety Pathophysiology: A DNA Methylation and Histone Modification Focused Review (2023) · cites this paper as Bannister and Kouzarides, 2011
D-2-hydroxyglutarate (D2HG) inhibits numerous demethylases, leading to changes in genomic and transcriptomic methylation profiles as well as gene expression and genome topology.
“D-2-hydroxyglutarate (D2HG) is one such oncometabolite, which inhibits numerous demethylases, leading to changes in genomic and transcriptomic methylation profiles as well as gene expression and genome topology 32,90-92 .”
From The roles of DNA, RNA and histone methylation in ageing and cancer (2019) · cites this paper as [32]
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- Authors
- Bannister, A. J., & Kouzarides, T.
- Affiliations
- University of Cambridge (GB)
- Corresponding author
- Kouzarides, Tony
- Venue
- Cell Research
- Published
- 2011-02-15
- Volume
- 21
- Issue
- 3
- Pages
- 381-395
- ISSN
- 1001-0602 (ISSN-L)
- 1748-7838
- PMC
- PMC3193420
- OpenAlex
- W2147524392
- Cited by
- 6,012
- References
- 130
- Citations by year
- 2026: 322 · 2025: 536 · 2024: 558 · 2023: 510 · 2022: 523 · 2021: 490 · 2020: 502 · 2019: 427 · 2018: 404 · 2017: 383 · 2016: 348 · 2015: 283 · 2014: 253 · 2013: 219 · 2012: 176
- FWCI
- 20.90
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Cell Research (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chromatin Remodeling and Cancer
- Keywords
- chromatin regulation, histone modifications, transcriptional regulation, epigenetics
- MeSH terms
- Chromatin, Heterochromatin, Histones, Protein Processing, Post-Translational, Histone Demethylases
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