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PRMT1 is the predominant type I protein arginine methyltransferase in mammalian cells.

Authors
Tang, J; Frankel, A; Cook, RJ; Kim, S; Paik, WK; Williams, KR; Clarke, S; Herschman, HR
Citation
The Journal of biological chemistry, 275(11):7723-7730, 2000
Journal Title
The Journal of biological chemistry
ISSN
0021-92581083-351X
Abstract
Type I protein arginine methyltransferases catalyze the formation of asymmetric omega-N(G),N(G)-dimethylarginine residues by transferring methyl groups from S-adenosyl-L-methionine to guanidino groups of arginine residues in a variety of eucaryotic proteins. The predominant type I enzyme activity is found in mammalian cells as a high molecular weight complex (300-400 kDa). In a previous study, this protein arginine methyltransferase activity was identified as an additional activity of 10-formyltetrahydrofolate dehydrogenase (FDH) protein. However, immunodepletion of FDH activity in RAT1 cells and in murine tissue extracts with antibody to FDH does not diminish type I methyltransferase activity toward the methyl-accepting substrates glutathione S-transferase fibrillarin glycine arginine domain fusion protein or heterogeneous nuclear ribonucleoprotein A1. Similarly, immunodepletion with anti-FDH antibody does not remove the endogenous methylating activity for hypomethylated proteins present in extracts from adenosine dialdehyde-treated RAT1 cells. In contrast, anti-PRMT1 antibody can remove PRMT1 activity from RAT1 extracts, murine tissue extracts, and purified rat liver FDH preparations. Tissue extracts from FDH(+/+), FDH(+/-), and FDH(-/-) mice have similar protein arginine methyltransferase activities but high, intermediate, and undetectable FDH activities, respectively. Recombinant glutathione S-transferase-PRMT1, but not purified FDH, can be cross-linked to the methyl-donor substrate S-adenosyl-L-methionine. We conclude that PRMT1 contributes the major type I protein arginine methyltransferase enzyme activity present in mammalian cells and tissues.
MeSH terms
AnimalsArginine/*metabolismMethylationMiceMice, Mutant StrainsOxidoreductases Acting on CH-NH Group Donors/genetics/isolation & purification/*metabolismProtein Methyltransferases/classification/isolation & purification/*metabolismProtein Processing, Post-TranslationalProtein-Arginine N-Methyltransferases/classification/isolation & purification/*metabolismRatsS-Adenosylmethionine/metabolism
PMID
10713084
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Journal Papers > School of Medicine / Graduate School of Medicine > Biochemistry & Molecular Biology
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