Lysine benzoylation is a histone mark regulated by SIRT2

He Huang, Di Zhang, Yi Wang, Mathew Perez-Neut, Zhen Han, Y. George Zheng, Quan Hao and Yingming Zhao ()
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He Huang: The University of Chicago
Di Zhang: The University of Chicago
Yi Wang: University of Hong Kong
Mathew Perez-Neut: The University of Chicago
Zhen Han: University of Georgia
Y. George Zheng: University of Georgia
Quan Hao: University of Hong Kong
Yingming Zhao: The University of Chicago

Nature Communications, 2018, vol. 9, issue 1, 1-11

Abstract: 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.

Date: 2018
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DOI: 10.1038/s41467-018-05567-w

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