Histone propionylation is a mark of active chromatin

Autor: Raphaël Margueron, Robert H. Schneider, Aaron Taudt, Anna Nieborak, Florian Richter, Marijke P. Baltissen, Helena de Fatima Magliarelli, Gergö Meszaros, Maria Colomé-Tatché, Sylvain Daujat, Michiel Vermeulen, Lara Zorro Shahidian, Stéphanie Le Gras, Gerhard Mittler, Diana Aguilar Gómez, Adam Fiseha Kebede, Romeo Ricci
Přispěvatelé: Stem Cell Aging Leukemia and Lymphoma (SALL)
Rok vydání: 2017
Předmět:
0301 basic medicine
Transcription
Genetic
PROTEIN
Histones
Mice
0302 clinical medicine
Structural Biology
Histone code
TRANSCRIPTION
RNA
Small Interfering
Histone Acetyltransferases
GENE-EXPRESSION
biology
Chemistry
Proteomics and Chromatin Biology
Chromatin
Cell biology
GENOME
Histone
Histone methyltransferase
MCF-7 Cells
RNA Interference
BUTYRYLATION
lipids (amino acids
peptides
and proteins)
ACETYLATION
RNA-POLYMERASE-II
complex mixtures
03 medical and health sciences
Histone H3
Protein Domains
Histone H1
Cell Line
Tumor
Histone H2A
Animals
Humans
Molecular Biology
COMPLEX
Mice
Inbred C57BL
HEK293 Cells
RAW 264.7 Cells
RECONSTITUTION
030104 developmental biology
biology.protein
METABOLIC-REGULATION
Acyl Coenzyme A
Protein Processing
Post-Translational
030217 neurology & neurosurgery
HeLa Cells
Zdroj: Nature Structural & Molecular Biology, 24, 12, pp. 1048-1062
Nature Structural & Molecular Biology, 24(12), 1048-1056. Nature Publishing Group
Nature Structural & Molecular Biology, 24, 1048-1062
ISSN: 1545-9993
Popis: 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.
Databáze: OpenAIRE
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