Histone H3 globular domain acetylation identifies a new class of enhancers

Madapura M Pradeepa, Graeme R Grimes, Yatendra Kumar, Gabrielle Olley, Gillian C A Taylor, Robert Schneider, Wendy A. Bickmore

Research output: Contribution to journalArticlepeer-review

Abstract / Description of output

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.
Original languageEnglish
Pages (from-to)681–686
Number of pages6
JournalNature Genetics
Issue number6
Early online date18 Apr 2016
Publication statusPublished - Jun 2016


Dive into the research topics of 'Histone H3 globular domain acetylation identifies a new class of enhancers'. Together they form a unique fingerprint.

Cite this