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Histone H3 globular domain acetylation identifies a new class of enhancers
Open accessAbstract
Histone acetylation is generally associated with active chromatin, but most studies have focused on the acetylation of histone tails. Various histone H3 and H4 tail acetylations mark the promoters of active genes. These modifications include acetylation of histone H3 at lysine 27 (H3K27ac), which blocks Polycomb-mediated trimethylation of H3K27 (H3K27me3). H3K27ac is also widely used to identify active enhancers, and the assumption has been that profiling H3K27ac is a comprehensive way of cataloguing the set of active enhancers in mammalian cell types. Here we show that acetylation of lysine residues in the globular domain of histone H3 (lysine 64 (H3K64ac) and lysine 122 (H3K122ac)) marks active gene promoters and also a subset of active enhancers. Moreover, we find a new class of active functional enhancers that is marked by H3K122ac but lacks H3K27ac. This work suggests that, to identify enhancers, a more comprehensive analysis of histone acetylation is required than has previously been considered.
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“For example, enhancers devoid of the classic H3K27ac mark have recently been described [163]; consistent with this, it was shown that this mark is not required for enhancer function, at least in mouse ESCs [164].”
From Transcriptional enhancers and their communication with gene promoters (2021) · cites this paper as [163]
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Metadata
- Authors
- Pradeepa, M. M., Grimes, G. R., Kumar, Y., Olley, G., Taylor, G. C. A., Schneider, R., & Bickmore, W. A.
- Affiliations
- University of Essex (GB)
- Institute of Genetics and Cancer (GB)
- Centre National de la Recherche Scientifique (FR)
- Corresponding author
- Pradeepa, Madapura M
- Bickmore, Wendy A
- ORCID
- Venue
- Nature Genetics
- Published
- 2016-04-18
- Volume
- 48
- Issue
- 6
- Pages
- 681-686
- ISSN
- 1061-4036 (ISSN-L)
- 1546-1718
- PMC
- PMC4886833
- OpenAlex
- W2342153705
- Cited by
- 240
- References
- 47
- Citations by year
- 2026: 19 · 2025: 22 · 2024: 18 · 2023: 22 · 2022: 22 · 2021: 24 · 2020: 36 · 2019: 27 · 2018: 21 · 2017: 21 · 2016: 7
- FWCI
- 13.17
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Genetics (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Open Access at Essex (University of Essex) (acceptedVersion)
- Edinburgh Research Explorer (University of Edinburgh) (submittedVersion, other-oa)
- HAL (submittedVersion)
- Site cant be reached (submittedVersion)
- PuSH - Publication Server of Helmholtz Zentrum München (submittedVersion)
- Queen Mary Research Online (Queen Mary University of London) (submittedVersion)
- Funders
- Agence Nationale de la Recherche
- Institut National de la Santé et de la Recherche Médicale
- Fondation pour la Recherche Médicale
- Medical Research Council
- FP7 Ideas: European Research Council (249956)
- 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
- histone acetylation, H3K27ac, enhancers, promoter, chromatin modification, embryonic stem cells, cancer cell lines, enhancer identification
- MeSH terms
- Acetylation, Enhancer Elements, Genetic, Gene Expression Regulation, Histones, Humans, Lysine, K562 Cells, Chromatin Immunoprecipitation, Embryonic Stem Cells
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