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Kebede, A.F.* ; Nieborak, A. ; Shahidian, L.Z. ; Le Gras, S.* ; Richter, F.M.* ; Gomez, D.A. ; Baltissen, M.P.* ; Meszaros, G.* ; Magliarelli, H.F.* ; Taudt, A. ; Margueron, R.* ; Colomé-Tatché, M. ; Ricci, R.* ; Daujat, S.* ; Vermeulen, M.* ; Mittler, G.* ; Schneider, R.

Histone propionylation is a mark of active chromatin.

Nat. Struct. Mol. Biol. 24, 1048–1056 (2017)
Verlagsversion Forschungsdaten DOI PMC
Open Access Gold
Histones are highly covalently modified, but the functions of many of these modifications remain unknown. In particular, it is unclear how histone marks are coupled to cellular metabolism and how this coupling affects chromatin architecture. We identified histone H3 Lys14 (H3K14) as a site of propionylation and butyrylation in vivo and carried out the first systematic characterization of histone propionylation. We found that H3K14pr and H3K14bu are deposited by histone acetyltransferases, are preferentially enriched at promoters of active genes and are recognized by acylation-state-specific reader proteins. In agreement with these findings, propionyl-CoA was able to stimulate transcription in an in vitro transcription system. Notably, genome-wide H3 acylation profiles were redefined following changes to the metabolic state, and deletion of the metabolic enzyme propionyl-CoA carboxylase altered global histone propionylation levels. We propose that histone propionylation, acetylation and butyrylation may act in combination to promote high transcriptional output and to couple cellular metabolism with chromatin structure and function.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Schlagwörter Rna-polymerase-ii; Metabolic-regulation; Gene-expression; Transcription; Acetylation; Complex; Protein; Genome; Reconstitution; Butyrylation
Sprache englisch
Veröffentlichungsjahr 2017
HGF-Berichtsjahr 2017
ISSN (print) / ISBN 1545-9993
e-ISSN 1545-9985
Zeitschrift Nature Structural & Molecular Biology
Quellenangaben Band: 24, Heft: 12, Seiten: 1048–1056 Artikelnummer: , Supplement: ,
Verlag Nature Publishing Group
Verlagsort New York, NY
Begutachtungsstatus Peer reviewed
Institut(e) Institute of Functional Epigenetics (IFE)
Institute of Computational Biology (ICB)
POF Topic(s) 30203 - Molecular Targets and Therapies
30205 - Bioengineering and Digital Health
Forschungsfeld(er) Helmholtz Diabetes Center
Enabling and Novel Technologies
PSP-Element(e) G-502800-001
G-503800-001
G-554200-001
PubMed ID 29058708
DOI 10.1038/nsmb.3490
WOS ID WOS:000417281800008
Erfassungsdatum 2017-11-10
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