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The metabolite methylglyoxal-mediated gene expression is associated with histone methylglyoxalation

ABSTRACT: The metabolite methylglyoxal-mediated gene expression is associated with histone methylglyoxalation

PROVIDER: PRJNA511620 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR8367730.fastq.gz	Fastqsanger.gz
	SRR8367740.fastq.gz	Fastqsanger.gz
	SRR8367750.fastq.gz	Fastqsanger.gz
	SRR8367721.fastq.gz	Fastqsanger.gz
	SRR8367731.fastq.gz	Fastqsanger.gz

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The metabolite methylglyoxal-mediated gene expression is associated with histone methylglyoxalation

Project description:RNA-seq analysis of Arabidopsis wild-type, glyI2, 35S::GLYI2 35S::GLYII4 seedlings suggested that MG mediates salt stress responsive gene expression. ChIP-seq analysis of MG-treated Arabidopsis wild-type seedlings with anti-MMP and anti-H3K4MG suggested that MG-mediated gene expression is associated with histone methylglyoxalation.

2021-01-05 | GSE124328 | GEO

The metabolite methylglyoxal-mediated gene expression is associated with histone methylglyoxalation.

Project description:Methylglyoxal (MG) is a byproduct of glycolysis that functions in diverse mammalian developmental processes and diseases and in plant responses to various stresses, including salt stress. However, it is unknown whether MG-regulated gene expression is associated with an epigenetic modification. Here we report that MG methylglyoxalates H3 including H3K4 and increases chromatin accessibility, consistent with the result that H3 methylglyoxalation positively correlates with gene expression. Salt stress also increases H3 methylglyoxalation at salt stress responsive genes correlated to their higher expression. Following exposure to salt stress, salt stress responsive genes were expressed at higher levels in the Arabidopsis glyI2 mutant than in wild-type plants, but at lower levels in 35S::GLYI2 35S::GLYII4 plants, consistent with the higher and lower MG accumulation and H3 methylglyoxalation of target genes in glyI2 and 35S::GLYI2 35S::GLYII4, respectively. Further, ABI3 and MYC2, regulators of salt stress responsive genes, affect the distribution of H3 methylglyoxalation at salt stress responsive genes. Thus, MG functions as a histone-modifying group associated with gene expression that links glucose metabolism and epigenetic regulation.

| S-EPMC7913762 | biostudies-literature

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Project description:Abstract Methylglyoxal is a highly reactive metabolite that is formed spontaneously in the glycolytic pathway. The side chains of various amino acid residues react with methylglyoxal to form advanced-glycation end products (AGEs). This enzyme-independent process introduces post-translational modifications (PTMs) onto the proteins and it was long thought that the resulting AGEs primarily inhibited proteins. More recent studies have shown that these AGEs can act in signaling and feedback loops. Moreover, it was shown that a large number of proteins react reversibly with methylglyoxal. These findings led to a renewed interest in methylglyoxal induced AGEs and led to the development of novel tools and methodologies that can be used to identify the modified proteins. Many of studies are nowadays still performed by adding methylglyoxal exogenously, often in a high concentration, despite the high reactivity of methylglyoxal. We here report new photocaged-methylglyoxal derivatives that allow the direct release of methylglyoxal in the sample of interest at the desired time and experimental condition. We demonstrate that the methylglyoxal derivatives can be released in situ by irradiating the photocaged probe with UV light. Furthermore, we show that this approach is more efficient. A far larger number of proteins are labeled with the photocaged probes than with the chemically activated probes. The here reported approach should allow studying in situ glycation under physiological more relevant conditions.

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Project description:The pathogenesis of cancer is rather complicated and includes multiple aspects, with metabolic reprogramming and angiogenesis as the leading hallmark characteristics. Recent reports have unveiled that the glycolytic metabolite lactate could modify histone lactylation level to epigenetically regulate gene expressions and biological processes in cancer, while the role of lactate-mediated histone lactylation in tumor angiogenesis remains elusive. By taking advantage of melanoma as the model, we demonstrate that lactate-mediated histone lactylation promotes tumor angiogenesis via IL-33/ST2 axis.

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Project description:Cancer Associated Histone Mutations

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Hypoxia-mediated regulation of histone demethylases affects angiogenesis associated functions in endothelial cells

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Cell envelope maintenance by PhoP is essential for Mycobacterium tuberculosis methylglyoxal resistance

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Project description:We have analyzed the genome-wide redistribution of RNA polymerase in E.coli upon methylglyoxal stress. Herefore, we have used ChIP-chip against the beta subunit of RNA polymerase and we have assessed changes in RNA polymerase distribution upon sub-lethal and lethal concentrations of methylglyoxal.

2011-12-15 | E-MTAB-100 | biostudies-arrayexpress

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