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Phosphorylation of histone H3.3 at serine 31 promotes p300 activity and enhancer acetylation.

Abstract：

:The histone variant H3.3 is enriched at enhancers and active genes, as well as repeat regions such as telomeres and retroelements, in mouse embryonic stem cells (mESCs)1-3. Although recent studies demonstrate a role for H3.3 and its chaperones in establishing heterochromatin at repeat regions4-8, the function of H3.3 in transcription regulation has been less clear9-16. Here, we find that H3.3-specific phosphorylation17-19 stimulates activity of the acetyltransferase p300 in trans, suggesting that H3.3 acts as a nucleosomal cofactor for p300. Depletion of H3.3 from mESCs reduces acetylation on histone H3 at lysine 27 (H3K27ac) at enhancers. Compared with wild-type cells, those lacking H3.3 demonstrate reduced capacity to acetylate enhancers that are activated upon differentiation, along with reduced ability to reprogram cell fate. Our study demonstrates that a single amino acid in a histone variant can integrate signaling information and impact genome regulation globally, which may help to better understand how mutations in these proteins contribute to human cancers20,21.

journal_name

Nat Genet

journal_title

Nature genetics

authors

Martire S,Gogate AA,Whitmill A,Tafessu A,Nguyen J,Teng YC,Tastemel M,Banaszynski LA

doi

10.1038/s41588-019-0428-5

subject

Has Abstract

pub_date

2019-06-01 00:00:00

pages

941-946

issue

6

eissn

1061-4036

issn

1546-1718

pii

10.1038/s41588-019-0428-5

journal_volume

51

pub_type

信件

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