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di Cerbo, V.* ; Mohn, F.* ; Ryan, D.P.* ; Montellier, E.* ; Kacem, S.* ; Tropberger, P.* ; Kallis, E.* ; Holzner, M.* ; Hoerner, L.* ; Feldmann, A.* ; Richter, F.M.* ; Bannister, A.J.* ; Mittler, G.* ; Michaelis, J.* ; Khochbin, S.* ; Feil, R.* ; Schuebeler, D.* ; Owen-Hughes, T.* ; Daujat, S.* ; Schneider, R.*

Acetylation of histone H3 at lysine 64 regulates nucleosome dynamics and facilitates transcription.

eLife 3:e01632 (2014)
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Post-translational modifications of proteins have emerged as a major mechanism for regulating gene expression. However, our understanding of how histone modifications directly affect chromatin function remains limited. In this study, we investigate acetylation of histone H3 at lysine 64 (H3K64ac), a previously uncharacterized acetylation on the lateral surface of the histone octamer. We show that H3K64ac regulates nucleosome stability and facilitates nucleosome eviction and hence gene expression in vivo. In line with this, we demonstrate that H3K64ac is enriched in vivo at the transcriptional start sites of active genes and it defines transcriptionally active chromatin. Moreover, we find that the p300 co-activator acetylates H3K64, and consistent with a transcriptional activation function, H3K64ac opposes its repressive counterpart H3K64me3. Our findings reveal an important role for a histone modification within the nucleosome core as a regulator of chromatin function and they demonstrate that lateral surface modifications can define functionally opposing chromatin states.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Schlagwörter Acetylation ; Chromatin ; Histone
ISSN (print) / ISBN 2050-084X
e-ISSN 2050-084X
Zeitschrift eLife
Quellenangaben Band: 3, Heft: , Seiten: , Artikelnummer: e01632 Supplement: ,
Verlag eLife Sciences Publications
Begutachtungsstatus Peer reviewed