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Lysine benzoylation is a novel histone mark [RNA-seq]

ABSTRACT: Lysine benzoylation is a novel histone mark [RNA-seq]

PROVIDER: PRJNA427337 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR6413160.fastq.gz	Fastqsanger.gz
	SRR6413161.fastq.gz	Fastqsanger.gz
	SRR6413162.fastq.gz	Fastqsanger.gz
	SRR6413163.fastq.gz	Fastqsanger.gz
	SRR6413164.fastq.gz	Fastqsanger.gz

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Lysine benzoylation is a novel histone mark

Project description:Lysine benzoylation is a novel histone mark

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Lysine benzoylation is a novel histone mark [ChIP-seq]

Project description:Lysine benzoylation is a novel histone mark [ChIP-seq]

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Lysine benzoylation is a novel histone mark [RNA-seq]

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.

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Lysine benzoylation is a novel histone mark [ChIP-seq]

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Metabolic Regulation of Gene Expression by Histone Lysine Ã-hydroxybutyrylation [RNA-seq]

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.

2016-04-06 | E-GEOD-69616 | biostudies-arrayexpress

Lysine benzoylation - 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.

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Project description:Patterning of DNA methylation in eukaryotic genomes is shaped by de novo methylation, maintenance mechanisms, and demethylation pathways, but how these processes interface with epigenetic modification of histones is poorly understood. We found that the targeting of histone H3 lysine four trimethylation (H3K4me3) with the catalytic domain of the SDG2 histone methyltransferase potently erased DNA methylation and gene silencing at FWA and other genes, and also erased CG DNA methylation in the transcribed region of genes. This methylation erasure was completely blocked in the ros1 dml2 dml3 triple mutant which eliminates DNA demethylation enzymes, showing that H3K4me3 promotes the active removal of DNA methylation rather than preventing CG methylation maintenance. We also found that targeting the removal of H3K4me3 with the novel protein TRBIP1, which acts in part by recruiting the H3K4me3 demethylase JMJ14, causes potent gene silencing. Furthermore, using a CRISPR-based system to simultaneously target both TRBIP1 and a CG specific DNA methyltransferase, we observed more potent establishment of DNA methylation and gene silencing than targeting the DNA methyltransferase by itself. These results highlight H3K4me3 as a potent anti-DNA methylation mark, and reveal potent and specific tools for epigenome engineering.

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