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Histone H3 globular domain acetylation identifies a new class of enhancers

Pradeepa, MM and Grimes, GR and Kumar, Y and Olley, G and Taylor, GCA and Schneider, R and Bickmore, WA (2016) 'Histone H3 globular domain acetylation identifies a new class of enhancers.' Nature Genetics, 48 (6). 681 - 686. ISSN 1061-4036

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Abstract

© 2016 Nature America, Inc. 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.

Item Type: Article
Subjects: Q Science > QH Natural history > QH426 Genetics
Divisions: Faculty of Science and Health > Life Sciences, School of
Depositing User: Jim Jamieson
Date Deposited: 16 May 2016 14:42
Last Modified: 22 Aug 2019 14:15
URI: http://repository.essex.ac.uk/id/eprint/16688

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