期刊
NATURE GENETICS
卷 48, 期 6, 页码 681-+出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/ng.3550
关键词
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资金
- Medical Research Council UK
- European Research Council advanced grant [249956]
- Fondation pour la Recherche Medicale (FRM)
- Agence Nationale de Recherche (ANR)
- La Ligue National Contre La Cancer (Equipe Labellise)
- INSERM Plan Cancer (Epigenetique et Cancer)
- Agence Nationale de Recherche (CoreAc)
- MRC [MC_PC_U127527202] Funding Source: UKRI
- European Research Council (ERC) [249956] Funding Source: European Research Council (ERC)
- Medical Research Council [MC_PC_U127527202, 1584120] Funding Source: researchfish
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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