Year: 2018
Type: article
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 (K bz ). Our study identifies 22 K bz 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 K bz 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 K bz 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.
Source: Nature Communications
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: gold
Estimated APC paid: $6,990
Awards: G1562951895, Re-Engineering Translational Research at the University of Chicago, G3884611229, G3946400285, Systems-wide analysis of histone lysine 2-hydroxyisobutyrylation pathway, G7100489832, SIRT6 and lysine fatty acylation in macrophage inflammation, G8077630019, University of Chicago Initiative for Maximizing Student Development (IMSD) - Renewal 01, G9000334782
OpenAlex ID: W2886279431