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Mina53 regulates the neural stem cell pool by acting as an arginine demethylase

ABSTRACT: Mina53 regulates the neural stem cell pool by acting as an arginine demethylase

PROVIDER: PRJNA1012474 | ENA |

REPOSITORIES: ENA

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Mina53 regulates the neural stem cell pool by acting as an arginine demethylase

Project description:To investigate the function Mina53 in the regulation of neural stem cells proliferation and differentiation, we collect neural stem cells which Mina53 has been knocked down by shRNA.

2024-05-20 | GSE242238 | GEO

Mina53 demethylates histone 4 arginine 3 asymmetric di-methylation to regulate neural stem/progenitor cell identity

Project description:Arginine methylation of histones plays a critical role in regulating gene expression. The writers (methyltransferases) and readers of methylarginine marks are well-known, but the erasers－arginine demethylases－remain mysterious. Here we identify Myc-induced nuclear antigen 53 (Mina53), a jumonji C domain containing protein, as an arginine demethylase for removing asymmetric di-methylation at arginine 3 of histone H4 (H4R3me2a). Using photoaffinity capture method, we first identified Mina53 as an interactor of H4R3me2a. Biochemical assays in vitro and in cells characterized the arginine demethylation activity of Mina53. Molecular dynamics simulations provide further atomic-level evidence that Mina53 acts on H4R3me2a. In a transgenic mouse model, specific Mina53 deletion in neural stem/progenitor cells prevented H4R3me2a demethylation at distinct genes clusters, dysregulating genes important for neural stem/progenitor cell proliferation and differentiation, and consequently impairing the cognitive function of mice. Collectively, we identify Mina53 as a bona fide H4R3me2a eraser, expanding the understanding of epigenetic gene regulation.

2024-10-22 | PXD045247 | Pride

Mina53 regulates the neural stem cell pool by acting as an argnine demethlysae

2024-05-20 | GSE232829 | GEO

Mina53 regulates the neural stem cell pool by acting as an argnine demethlysae

Project description:Mina53 regulates the neural stem cell pool by acting as an argnine demethlysae

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Genes regulated by Mina53 in Mina53-KO NSPCs compared with wild-type NSPCs.

Project description:In order to investigate the role of Mina53 in the NSPC proliferation and differentiation, we performed RNA-seq using Mina53-KO NSPCs and wild-type NSPCs.

2024-11-14 | GSE275270 | GEO

Genes enriched with H4R3me2a modification in Mina53-KO NSPCs compared with wild-type NSPCs.

Project description:In order to investigate the role of Mina53 in the NSPC proliferation and differentiation, we performed CUT-TAG using anti-H4R3me2a antibody in Mina53-KO NSPCs and wild-type NSPCs.

2024-11-14 | GSE277857 | GEO

Histone arginine demethylation by RDMe1

Project description:Histone methylation mainly occurs on lysine and arginine residues. While lysine methylation can be removed by LSD1 and JmjC domain-containing demethylases, the existence of histone arginine demethylases is highly controversial. Here, we performed a high-content cell-based screening of a cDNA library containing 2,500 nuclear proteins and identified RDMe1 as a histone arginine demethylase. Overexpression of RDMe1 in HEK293T cells reduces H3R2me1/2a and H4R3me1/2a levels. In vitro, RDMe1 specifically demethylates H3R2me1/2a and H4R3me1/2a, and generates formaldehyde and succinate. The enzymatic activity requires Fe(II) and α-ketoglutarate as cofactors. RDMe1 is mainly located in the nucleolar and regulates rRNA transcription by demethylating H3R2me2a. ChIP-seq reveals that RDMe1 demethylates H4R3me2a in the promoter in a genome-wide scale. NMR reveals that RDMe1 binds iron and substrate peptides with N and C termini, respectively. Mutation of the iron binding residues abolished the binding and the demethylase activity. Thus, we identify a histone arginine demethylase and reveal the reversibility of arginine methylation.

2022-01-09 | GSE124890 | GEO

Genes regulated by Mina53 in Mina53-KO NSPCs compared with wild-type NSPCs.

Project description:Genes regulated by Mina53 in Mina53-KO NSPCs compared with wild-type NSPCs.

| PRJNA1150155 | ENA

Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis

Project description:Reversible protein phosphorylation is an important and ubiquitous protein modification in all living cells. We report that protein arginine phosphorylation plays a physiological significant role for the regulation of protein activity. We detected 121 arginine phospho-sites for 87 proteins in the Gram-positive model organism Bacillus subtilis in vivo. Moreover, we provide evidences that arginine phosphorylations are involved in the fine-tuned signal transduction of many critical cellular processes, such as protein degradation, motility, competence, stringent and stress response. Our results suggest that in B. subtilis the activity of a protein arginine phosphatase allows a fast regulation of protein activity by protein arginine kinases and that protein arginine phosphorylations play an important role as a reversible post-translational modification in bacteria. Cells were grown under vigorous agitation at 37 M-BM-0C in a defined medium (StM-CM-<lke et al., 1993, J Gen Microbiol 139, 2041-2045). Samples were taken at OD500 0.4 and 1h upon entry into stationary phase. Microarray hybridizations were performed with RNA from three biological replicates. The individual samples were labeled with Cy5; a reference pool containing equal amounts of RNA from all 10 samples was labeled with Cy3.

2012-03-31 | E-GEOD-31249 | biostudies-arrayexpress

Histone methylation profiles of H3K4me3, H3K27me3, H3K9me3, and H3R8me2a in WT and mdig/mina53 KO BEAS-2B cells

Project description:The mineral dust-induced gene (mdig) is overexpressed in a number of human cancers, suggesting critical roles of this gene played on the pathogenesis of cancers. Unlike several other JmjC-domain containing proteins that exhibit histone demethylase activity, it remains enigmatic whether mdig is involved in the demethylation processes of the histone proteins. To provide direct evidence suggesting contribution of mdig to the demethylation of histone proteins, we report the global histone methylation profile of H3K4me3, H3K27me3, H3K9me3, and H3R8me2a in human bronchial epithelial BEAS-2B cells with mina53/mdig knockout. ChIP-seq revealed a pronounced increase of the repressive histone trimethylation with mdig depletion, including H3K9me3 and H3K27me3. Data from both ChIP-seq and RNA-seq suggested that genetic disruption of mdig enriches repressive histone trimethylation and inhibits expression of target genes in the oncogenic pathways of cell growth, stemness of the cells, tissue fibrosis, and cell motility. Our study provides the first insight into the molecular effects of mdig as an antagonist for repressive histone methylation markers and suggests that targeting mdig may represent a new area to explore in cancer therapy.

2020-02-15 | GSE145354 | GEO

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