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Nat Genet. 2016 Jun;48(6):681-6. doi: 10.1038/ng.3550. Epub 2016 Apr 18.

Histone H3 globular domain acetylation identifies a new class of enhancers.

Author information

1
MRC Human Genetics Unit, MRC Institute of Genetics and Molecular Medicine at the University of Edinburgh, Edinburgh, UK.
2
School of Biological Sciences, University of Essex, Colchester, UK.
3
Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), CNRS UMR 7104, INSERM U964, Université de Strasbourg, Illkirch, France.
4
Helmholtz Zentrum München, Institute of Functional Epigenetics, Neuherberg, Germany.

Abstract

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.

PMID:
27089178
PMCID:
PMC4886833
DOI:
10.1038/ng.3550
[Indexed for MEDLINE]
Free PMC Article

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