01
Introduction to the background of the article
BACKGROUND INTRODUCTION
The chromatin structure and transcriptional activity of genes are regulated by post-translational modifications (PTM) of various proteins in histones (or histone marks). There is increasing evidence that histone modification status is associated with cellular metabolism. For example, cellular metabolism or intestinal microbial fermentation can produce short chain fatty acids such as crotonate, butyrate, alpha-ketoglutarate and 3-hydroxybutyrate. These metabolites can be used as precursors for the formation of acyl-CoA for histone acylation. These various acyl-CoAs offer an interesting possibility that there are likely to be unreported pathways in the body that regulate histone modifications through cell or flora metabolites to affect epigenetics.
Benzoyl-CoA is an intermediate in the degradation of a large number of aromatic growth substrates in bacteria and gut flora. In mammalian cells, a possible source of benzoyl-CoA is sodium benzoate (SB), one of the most commonly used preservatives in the world, with a maximum allowable concentration of up to 0.1% in food. Although SB has been classified as a "generally regarded as safe" by the US Food and Drug Administration (FDA), emerging research suggests that exposure to SB may cause harm to consumers. In addition, intravenous injection of excess SB can cause serious complications. These findings suggest that human health risks are associated with SB. However, the underlying biological mechanisms are still unknown.
Huang He et al. of the University of Chicago, starting with the novel modification of histone-labeled lysine benzoylation, discovered a new epigenetic mechanism that may lead to the above-mentioned adverse physiological responses of SB to humans. One of the reasons for this discovery was published in Nature Communications magazine ( IF2017-2018=12.353; Comprehensive Zone 2 ) in 2018, entitled "Lysine benzoylation is a histone mark regulated by SIRT2".
02
Main method used
METHODS
1. Western Blot (WB)
2. Liquid chromatography-mass spectrometry (HPLC-MS/MS)
3. Immunoprecipitation (IP)
4. Immunofluorescence staining
5. Binding Site Analysis (CHIP-seq)
6. Transcriptome sequencing technology (RNA-seq)
03
Summary of the main contents of the article
ABSTRACT
Histone modification can dynamically regulate the structure and function of chromatin and is closely related to various physiological and pathological processes. The recognition and characterization of histone labeling-lysine benzoylation (Kbz) is reported herein. In this study, 22 Kbz sites on histones were identified from HepG2 and RAW cells. Sodium benzoate (SB) is an FDA approved drug and is widely used as a chemical food preservative. Histone Kbz can be produced by sodium benzoate by producing benzoyl CoA. By ChIP-seq and RNA-seq analysis, this study demonstrates that histone Kbz markers are associated with gene expression and have a different physiological relevance than histone acetylation. In addition, studies have shown that SIRT2, an NAD + -dependent protein deacetylase, removes histone Kbz both in vitro and in vivo. Therefore, this study reveals a novel histone modification with potential physiological relevance, a finding that benzoic acid used as a chemical food preservative may also have unknown functions such as epigenetic modification regulation.
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