Lysine benzoylation is a histone mark regulated by SIRT2

Nature Communications
He HuangYingming Zhao

Abstract

Metabolic regulation of histone marks is associated with diverse biological processes through dynamically modulating chromatin structure and functions. Here we report the identification and characterization of a histone mark, lysine benzoylation (Kbz). Our study identifies 22 Kbz sites on histones from HepG2 and RAW cells. This type of histone mark can be stimulated by sodium benzoate (SB), an FDA-approved drug and a widely used chemical food preservative, via generation of benzoyl CoA. By ChIP-seq and RNA-seq analysis, we demonstrate that histone Kbz marks are associated with gene expression and have physiological relevance distinct from histone acetylation. In addition, we demonstrate that SIRT2, a NAD+-dependent protein deacetylase, removes histone Kbz both in vitro and in vivo. This study therefore reveals a new type of histone marks with potential physiological relevance and identifies possible non-canonical functions of a widely used chemical food preservative.

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Datasets Mentioned

BETA
PXD010332

Methods Mentioned

BETA
ChIP-seq
immunoprecipitation
RNA-seq
acetylation
dot blot
acylation
transfection
ChIP
electrophoresis
PCR

Software Mentioned

GSEA
Bowtie 41
edgeR
Autodock
. plot
PyMol
PTMap
MaxQuant
LigPlot +
AutoDock vina

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