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In 2018, Professor Yingming Zhao of the University of Chicago reported the discovery of benzoylation, a novel acylation modification that contains a benzene ring. Benzoylation was found to occur on histones in response to sodium benzoate (NaBz) treatment, which produces benzoyl-CoA. The protein deacetylase Sirt2 was also found to possess benzoylase activity. Benzoylation is primarily located in the promoter region of genes and regulates gene expression levels, thus representing a novel area of research in the field of protein post-translational modification. The research findings were published in the journal Nature Communications.
The N-terminal tail of histone lysine is the main site of benzoylation modification. The modification group is larger (twice that of acetylation) and more hydrophobic (three times that of acetylation). Benzoylation modification has a greater structural impact than acetylation and has a more significant regulatory effect on genes, making it an area of interest for researchers. PTM BIO is currently the only company offering Pan benzoylation modified antibodies and benzoylation modified omics services, which can assist researchers in investigating the functional mechanisms of benzoylation.
1. Nat Commun：Lysine benzoylation is a histone mark regulated by SIRT2
In this study, researchers used benzoylation modification omics and biochemistry experiments to identify 22 lysines that can undergo Kbz modification on histones. This modification will be stimulated by sodium benzoate and regulated by sirt2. ChIP-seq and RNA-seq data reveal that Kbz modification is mainly concentrated on the promoter of the gene, and its physiological function is not the same as acetylation, which will affect the regulatory response of gene expression level.
2. Nucleic Acids Res: Histone benzoylation serves as an epigenetic mark for DPF and YEATS family proteins
In this study, with the help of the highly specific Kbz pan antibody provided by PTM BIO, the researchers confirmed that NaBz could induce the up regulation of histone Kbz signal in cells and animals, identified DPF and Yeats family proteins as "readers" of Kbz modification for the first time, and expounded in detail the molecular mechanism of differential recognition of Kbz modification by DPF and Yeats domains.
3. Nat Commun :Global profiling of regulatory elements in the histone benzoylation pathway
Researchers systematically studied the regulatory protein of histone Kbz in Saccharomyces cerevisiae, and identified the molecular mechanism of Kbz modifying enzyme (GCN5), modifying enzyme (Hst2), and recognizing protein (Taf14 and Sas5) through genetic, biochemical, and structural analysis. The authors also identified many non-histone proteins with Kbz modification through benzoylation modified proteomics, especially proteins involved in ribosome synthesis and metabolism. These research results laid a foundation for analyzing the role of Kbz in different cellular processes.
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