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Protein arginine methyltransferase PRMT1 is essential for palatogenesis

ABSTRACT: Protein arginine methyltransferase PRMT1 is essential for palatogenesis

PROVIDER: PRJNA472987 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR7215530_1.fastq.gz	Fastqsanger.gz
	SRR7215530_2.fastq.gz	Fastqsanger.gz
	SRR7215531_1.fastq.gz	Fastqsanger.gz
	SRR7215531_2.fastq.gz	Fastqsanger.gz
	SRR7215532_1.fastq.gz	Fastqsanger.gz

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The arginine methyltransferase PRMT1 establishes transcriptomic homeostasis essential for spermatogonial differentiation and male fertility

Project description:Protein arginine methyltransferase 1 (Prmt1) is known as the major Type-I protein arginine methyltransferase that deposits asymmetrical dimethylarginine (ADMA) in both histone and non-histone substrates. Nonetheless, how Prmt1 and its downstream signalling through substrate methylation function in the male germline development remains poorly understood. In this study, we discovered that Prmt1 is predominantly present in the spermatogonial population during mouse spermatogenesis. Using three Cre-mediated conditional Prmt1 knockout mouse lines, we observed that Prmt1 is essential for the maintenance of spermatogonial cells and Prmt1-deposited ADMA marks coordinate an inherent homeostasis among three types of substrate methylation. In conjunction with high-throughput Cut&Tag and modified mini-bulk Smart-seq2 analyses, we unveiled that Prmt1-mediated H4R3me2a mark enriched in the promoter region, together with other histone arginine methylations, drives a global transcriptomic landscape that maintains the regular gene expression and alternative splicing. Collectively, we provide the genetic evidence showing the essential role of Prmt1-deposited arginine methylation in the establishment of transcriptional homeostasis, and shed light on the methylarginine signalling pathway in orchestrating spermatogonial development in the mammalian germline.

2023-03-31 | GSE227857 | GEO

Protein arginine methyltransferase PRMT1 is essential for palatogenesis

Project description:We report that neural crest-specific deletion of Prmt1 caused craniofacial malformations including cleft palate.

2019-09-01 | GSE114894 | GEO

Protein Arginine Methyltransferase PRMT1 Is Essential for Palatogenesis.

Project description:Cleft palate is among the most common birth defects. Currently, only 30% of cases have identified genetic causes, whereas the etiology of the majority remains to be discovered. We identified a new regulator of palate development, protein arginine methyltransferase 1 (PRMT1), and demonstrated that disruption of PRMT1 function in neural crest cells caused complete cleft palate and craniofacial malformations. PRMT1 is the most highly expressed of the protein arginine methyltransferases, enzymes responsible for methylation of arginine motifs on histone and nonhistone proteins. PRMT1 regulates signal transduction and transcriptional activity that affect multiple signal pathways crucial in craniofacial development, such as the BMP, TGFβ, and WNT pathways. We demonstrated that Wnt1-Cre;Prmt1 fl/fl mice displayed a decrease in palatal mesenchymal cell proliferation and failure of palatal shelves to reach the midline. Further analysis in signal pathways revealed that loss of Prmt1 in mutant mice decreased BMP signaling activation and reduced the deposition of H4R3me2a mark. Collectively, our study demonstrates that Prmt1 is crucial in palate development. Our study may facilitate the development of a better strategy to interrupt the formation of cleft palate through manipulation of PRMT1 activity.

| S-EPMC6728548 | biostudies-literature

The arginine methyltransferase PRMT1 establishes transcriptomic homeostasis essential for spermatogonial differentiation and male fertility

Project description:The arginine methyltransferase PRMT1 establishes transcriptomic homeostasis essential for spermatogonial differentiation and male fertility

| PRJNA947190 | ENA

PRMT1-dependent Arginine methylation regulates replication stress response through DNA-protein kinase

Project description:PRMT1 is the major Arginine methyltransferase in mammalian cells and its over-expression in human cancer has been linked to poor response to cancer therapy. Here, combining mass spectrometry-based global methyl-proteomics with genome-wide mRNA expression profiling, we identify PRMT1 and its associated Arginine methylation as a regulatory hubs controlling cancer cell response to replicative stress agents. We show that DNA-PK binds to PRMT1 and regulates both its subcellular localization and activity, leading to PRMT1 recruitment to drug-stalled replication forks and channelling its methyl-transferase activity from its soluble targets towards Arginine 3 of histone H4. This DNA-PK-PRMT1 axis is required for the induction of the Senescence-Associated Secretory Phenotype, which sustains cell cycle arrest and protects cells from apoptosis. Our data show that Arginine-methylation regulates the adaptive response of cancer cell to replicative stress agents and might be targeted to sensitize cancer cells to genotoxic chemotherapeutics

2020-01-14 | GSE106609 | GEO

Toxoplasma gondii arginine methyltransferase 1 (PRMT1) regulates parasite counting during tachyzoite cell division

Project description:PRMT1 is thought to be responsible for the majority of PRMT activity in Toxoplasma gondii, but its exact function is unknown. We generated T. gondii mutants lacking PRMT1 (∆prmt1) by deletion of the PRMT1 gene. ∆prmt1 parasites exhibit morphological defects during cell division and grow slowly, and this phenotype reverses in the complemented strain ∆prmt::PRMT1mRFP. PRMT1 localizes primarily in the cytoplasm with enrichment at the centrosome, and the strain lacking PRMT1 is unable to segregate progeny accurately. Unlike wild-type and complemented parasites, ∆prmt1 parasites have abnormal daughter buds, perturbed centrosome stoichiometry, and loss of synchronous replication. Whole genome expression profiling demonstrated differences in expression of cell cycle regulated genes in ∆prmt1 relative to the complemented ∆prmt1::PRMT1mRFP and parental wild-type strains, but these changes did not correlate with a specific block in cell cycle. Although PRMT1’s primary biological function was previously proposed to be methylation of histones, our genetic studies suggest that the most critical function of PRMT1 is within the centrosome as a regulator of daughter cell counting to assure the proper replication of the parasite. RNA samples were isolated in triplicates from RH-hxgprt parent strain (W), PRMT1 knockout (K) strain and PRMT1 knockout strain complemented with RFP-tagged PRMT1 protein (C). Parasites were grown for 32h at 37C. Samples were hybridized to the Toxoplasma gondii Affymetrix microarray (ToxoGeneChip: http://ancillary.toxodb.org/docs/Array-Tutorial.html). Hybridization data was preprocessed with Robust Multi-array Average (RMA) and normalized using per chip and per gene median polishing and analyzed using the software package GeneSpring GX (Agilent Technologies).

2015-09-18 | E-GEOD-73177 | biostudies-arrayexpress

Prmt1 safeguards mouse embryonic stem cells against bias toward the extraembryonic endoderm cell fate via arginine methylation of Klf4

Project description:Heterogeneous gene expression is a characteristic feature of stem cells and is essential for steering lineage choices. However, the molecular mechanisms of heterogeneity remain largely unknown. Here, we report that depletion of protein arginine methyltransferase 1 (Prmt1) in mouse embryonic stem (ES) cells heterogeneously induces the expression of primitive endoderm (PrE) genes, consequently biasing the cells to fluctuate toward the extraembryonic endoderm stem (XEN) cell fate. Furthermore, the pluripotency factor Klf4 is arginine-methylated by Prmt1 at arginine 396 (R396), which is required for recruitment of the mSin3a/HDAC complex to silence PrE genes. Importantly, when methylation is disrupted by a Prmt1 knockout, a Prmt1 inhibitor, or a blocked methylation site in Klf4, ES cells are predisposed to XEN induction. Our data demonstrate the importance of Prmt1 in the fluctuating heterogeneity of ES cells and reveal a regulatory mechanism for cell fate decisions that is centered on Klf4 methylation mediated by Prmt1.

2021-12-27 | GSE124920 | GEO

Transcription profiling of human HeLa cells follwing siRNA mediated knock down of the arginine methyltransferases CARM1 and/or PRMT1

Project description:siRNA mediated knockdown of the arginine methyltransferases CARM1 and/or PRMT1 in HeLa cells

2007-08-30 | E-MEXP-1173 | biostudies-arrayexpress

Targeting Type I arginine methyltransferase PRMT1 promotes the T cell mediated antitumor immune response

Project description:Targeting Type I arginine methyltransferase PRMT1 promotes the T cell mediated antitumor immune response

| PRJNA682604 | ENA

Toxoplasma gondii arginine methyltransferase 1 (PRMT1) regulates parasite counting during tachyzoite cell division

2015-09-18 | GSE73177 | GEO