Fiche publication
Date publication
décembre 2017
Journal
Nature structural & molecular biology
Auteurs
Membres identifiés du Cancéropôle Est :
Pr RICCI Roméo
,
Dr DAUJAT Sylvain
Tous les auteurs :
Kebede AF, Nieborak A, Shahidian LZ, Le Gras S, Richter F, Gómez DA, Baltissen MP, Meszaros G, Magliarelli HF, Taudt A, Margueron R, Colomé-Tatché M, Ricci R, Daujat S, Vermeulen M, Mittler G, Schneider R
Lien Pubmed
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.
Mots clés
Acetylation, Acyl Coenzyme A, genetics, Animals, Cell Line, Tumor, Chromatin, metabolism, HEK293 Cells, HeLa Cells, Histone Acetyltransferases, metabolism, Histones, metabolism, Humans, MCF-7 Cells, Mice, Mice, Inbred C57BL, Protein Domains, Protein Processing, Post-Translational, physiology, RAW 264.7 Cells, RNA Interference, RNA, Small Interfering, genetics, Transcription, Genetic, genetics
Référence
Nat. Struct. Mol. Biol.. 2017 Dec;24(12):1048-1056
