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Histone H3 globular domain acetylation identifies a new class of enhancers.
Nat. Genet. 48, 681-686 (2016)
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(1). These modifications include acetylation of histone H3 at lysine 27 (H3K27ac), which blocks Polycomb-mediated trimethylation of H3K27 (H3K27me3)(2). H3K27ac is also widely used to identify active enhancers(3,4), 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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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
Embryonic Stem-cells; Human Genome; Transcription Factors; Super-enhancers; Lateral Surface; Sequencing Data; Genes; System; Signatures; Promoters
Language
Publication Year
2016
HGF-reported in Year
2016
ISSN (print) / ISBN
1061-4036
e-ISSN
1546-1718
Journal
Nature Genetics
Quellenangaben
Volume: 48,
Issue: 6,
Pages: 681-686
Publisher
Nature Publishing Group
Publishing Place
New York, NY
Reviewing status
Peer reviewed
Institute(s)
Institute of Functional Epigenetics (IFE)
POF-Topic(s)
30203 - Molecular Targets and Therapies
Research field(s)
Helmholtz Diabetes Center
PSP Element(s)
G-502800-001
DOI
10.1038/ng.3550
WOS ID
WOS:000376744200017
Erfassungsdatum
2016-06-27