Histone propionylation is a mark of active chromatin
2 HMGU - Helmholtz Zentrum München = German Research Center for Environmental Health
3 MPI-IE - Max Planck Institute of Immunobiology and Epigenetics
4 Goethe University Frankfurt = Goethe-Universität Frankfurt am Main
5 UNAM - Universidad Nacional Autónoma de México = National Autonomous University of Mexico
6 Radboud Institute for Molecular Life Sciences [Nijmegen, the Netherlands]
7 Laboratoire de Biochimie et de Biologie Moléculaire
8 ERIBA - European Research Institute for the Biology of Ageing [Groningen]
9 Institut Curie [Paris]
10 TUM - Technische Universität Munchen = Technical University Munich = Université Technique de Munich
11 LMU - Ludwig Maximilian University [Munich] = Ludwig Maximilians Universität München
- Fonction : Auteur
- PersonId : 770046
- IdHAL : stephanie-le-gras
- ORCID : 0000-0001-6293-6507
- IdRef : 258396687
- Fonction : Auteur
- PersonId : 1064607
- Fonction : Auteur
- PersonId : 1064608
- Fonction : Auteur
- PersonId : 1218552
- ORCID : 0000-0002-9093-7977
- Fonction : Auteur
- PersonId : 1151698
- IdHAL : romeo-ricci
- ORCID : 0000-0002-9766-4369
- IdRef : 189067950
- Fonction : Auteur
- PersonId : 1134657
- ORCID : 0000-0001-5107-119X
- IdRef : 250394758
Résumé
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.