Project description:We identified and characterized a previously undescribed histone mark, lysine benzoylation. This histone mark could be modulated 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 lysine benzoylation marks are involved in regulation of gene expression and associated with diverse biological processes. This study therefore reveals a new type of physiological relevant histone mark and identifies non-conical functions of a widely used chemical food preservative.
Project description:We identified and characterized a previously undescribed histone mark, lysine benzoylation. This histone mark could be modulated 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 lysine benzoylation marks are involved in regulation of gene expression and associated with diverse biological processes. This study therefore reveals a new type of physiological relevant histone mark and identifies non-conical functions of a widely used chemical food preservative.
Project description:We identified a new type of histone mark-lysine Ã-hydroxybutyrylation (Kbhb). This ketone body derived histone mark (Kbhb) was dramatically induced in livers during starvation. To charactize histopne Kbhb: 1) We mapped genomic distributions of histone Kbhb marks (H3K9bhb, H3K4bhb and H4K8bhb) by ChIP-seq in mouse liver. 2) We examined the response of histone Kbhb mark to starvation by carrying out ChIP-seq experiments for H3K9bhb in both "starved" and "fed" mouse liver. 3) We also examined differentially-expressed genes during starvation by carrying out RNA-seq experiments in both "starved" and "fed" mouse liver. By integrating analyses of ChIP-seq and RNA-seq data, we tried to get a correlation between H3K9bhb mark and gene expression in response to starvation. Sequencing was performed on the HiSeq2000 (Illumina). RNA-seq of mouse liver cells both in "starved" and "fed" conditions.
Project description: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), a FDA-approved drug and a widely used chemical food preservative, via generation of benzoyl CoA.
Project description: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), a FDA-approved drug and a widely used chemical food preservative, via generation of benzoyl CoA.
Project description:We identified a new type of histone mark-lysine ß-hydroxybutyrylation (Kbhb). This ketone body derived histone mark (Kbhb) was dramatically induced in livers during starvation. To charactize histopne Kbhb: 1) We mapped genomic distributions of histone Kbhb marks (H3K9bhb, H3K4bhb and H4K8bhb) by ChIP-seq in mouse liver. 2) We examined the response of histone Kbhb mark to starvation by carrying out ChIP-seq experiments for H3K9bhb in both "starved" and "fed" mouse liver. 3) We also examined differentially-expressed genes during starvation by carrying out RNA-seq experiments in both "starved" and "fed" mouse liver. By integrating analyses of ChIP-seq and RNA-seq data, we tried to get a correlation between H3K9bhb mark and gene expression in response to starvation. Sequencing was performed on the HiSeq2000 (Illumina).
Project description:Methylation of histone H3 lysine-79 is an epigenetic mark for gene regulation in development, cellular differentiation and disease progression. However, it remains poorly understood how this histone mark is translated into downstream effects due to the lack of knowledge of H3K79 methylation ‘readers’. Here, we develop a nucleosome-based photoaffinity probe to capture proteins that recognize H3K79 dimethylation (H3K79me2) in nucleosomal context. In combination with a quantitative proteomics approach, this probe identifies menin as a bona fide “reader” for H3K79me2. Menin directly and selectively binds to the nucleosome with H3K79me2 mark in vitro. In cells, menin is tightly associated with this histone mark on chromatin, particularly in gene bodies. Reading H3K79me2 at intragenic enhancers, menin promotes gene transcription, likely by mediating enhancer–promoter interactions.