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Nat Struct Mol Biol. 2017 Dec;24(12):1048-1056. doi: 10.1038/nsmb.3490. Epub 2017 Oct 23.

Histone propionylation is a mark of active chromatin.

Author information

1
Institut de Génétique et de Biologie Moléculaire et Cellulaire, Illkirch, France.
2
Max Planck Institute of Immunobiology and Epigenetics, Freiburg, Germany.
3
Institute of Functional Epigenetics, Helmholtz Zentrum München, Neuherberg, Germany.
4
Goethe-Universität Fachbereich Medizin, Frankfurt, Germany.
5
Undergraduate Program in Genomic Sciences, National Autonomous University of Mexico, Mexico City, Mexico.
6
Radboud University Nijmegen, Radboud Institute for Molecular Life Sciences, Nijmegen, the Netherlands.
7
Université de Strasbourg, Strasbourg, France.
8
Laboratoire de Biochimie et de Biologie Moléculaire, Nouvel Hôpital Civil, Strasbourg, France.
9
European Research Institute for the Biology of Ageing, University of Groningen, University Medical Center Groningen, Groningen, the Netherlands.
10
Institute of Computational Biology, Helmholtz Zentrum München, Neuherberg, Germany.
11
Institut Curie, Paris, France.
12
Technical University Munich, Freising, Germany.
13
Ludwig-Maximilains-Universität München, Faculty of Biology, Munich, Germany.

Abstract

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.

PMID:
29058708
DOI:
10.1038/nsmb.3490
[Indexed for MEDLINE]

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