RGD Reference Report - Arginine N-methyltransferase 1 is required for early postimplantation mouse development, but cells deficient in the enzyme are viable. - Rat Genome Database

RGD Reference Report - Arginine N-methyltransferase 1 is required for early postimplantation mouse development, but cells deficient in the enzyme are viable. - Rat Genome Database

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Arginine N-methyltransferase 1 is required for early postimplantation mouse development, but cells deficient in the enzyme are viable.
Authors:	Pawlak, MR Scherer, CA Chen, J Roshon, MJ Ruley, HE
Citation:	Pawlak MR, etal., Mol Cell Biol 2000 Jul;20(13):4859-69.
RGD ID:	737807
Pubmed:	PMID:10848611 (View Abstract at PubMed)
PMCID:	PMC85937 (View Article at PubMed Central)
Protein arginine N-methyltransferases have been implicated in a variety of processes, including cell proliferation, signal transduction, and protein trafficking. In this study, we have characterized essentially a null mutation induced by insertion of the U3betaGeo gene trap retrovirus into the second intron of the mouse protein arginine N-methyltransferase 1 gene (Prmt1). cDNAs encoding two forms of Prmt1 were characterized, and the predicted protein sequences were found to be highly conserved among vertebrates. Expression of the Prmt1-betageo fusion gene was greatest along the midline of the neural plate and in the forming head fold from embryonic day 7.5 (E7.5) to E8.5 and in the developing central nervous system from E8.5 to E13.5. Homozygous mutant embryos failed to develop beyond E6.5, a phenotype consistent with a fundamental role in cellular metabolism. However, Prmt1 was not required for cell viability, as the protein was not detected in embryonic stem (ES) cell lines established from mutant blastocysts. Low levels of Prmt1 transcripts (approximately 1% of the wild-type level) were detected as assessed by a quantitative reverse transcription-PCR assay. Total levels of arginine N-methyltransferase activity and asymmetric N(G), N(G)-dimethylarginine were reduced by 85 and 54%, respectively, while levels of hypomethylated substrates were increased 15-fold. Prmt1 appears to be a major type I enzyme in ES cells, and in wild-type cells, most substrates of the enzyme appear to be maintained in a fully methylated state.

Objects referenced in this article

Gene	PRMT1	protein arginine methyltransferase 1	Homo sapiens
Gene	Etfb	electron transferring flavoprotein, beta polypeptide	Mus musculus
Gene	Fut1	fucosyltransferase 1	Mus musculus
Gene	Il4i1	interleukin 4 induced 1	Mus musculus
Gene	Ldhc	lactate dehydrogenase C	Mus musculus
Gene	Prmt1	protein arginine N-methyltransferase 1	Mus musculus
Gene	Prmt1	protein arginine methyltransferase 1	Rattus norvegicus

Additional Information