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

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dc.contributor.authorTang, J-
dc.contributor.authorFrankel, A-
dc.contributor.authorCook, RJ-
dc.contributor.authorKim, S-
dc.contributor.authorPaik, WK-
dc.contributor.authorWilliams, KR-
dc.contributor.authorClarke, S-
dc.contributor.authorHerschman, HR-
dc.date.accessioned2011-07-27-
dc.date.available2011-07-27-
dc.date.issued2000-
dc.identifier.issn0021-9258-
dc.identifier.urihttp://repository.ajou.ac.kr/handle/201003/3612-
dc.description.abstractType 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.-
dc.language.isoen-
dc.subject.MESHAnimals-
dc.subject.MESHArginine-
dc.subject.MESHMethylation-
dc.subject.MESHMice-
dc.subject.MESHMice, Mutant Strains-
dc.subject.MESHOxidoreductases Acting on CH-NH Group Donors-
dc.subject.MESHProtein Methyltransferases-
dc.subject.MESHProtein Processing, Post-Translational-
dc.subject.MESHProtein-Arginine N-Methyltransferases-
dc.subject.MESHRats-
dc.subject.MESHS-Adenosylmethionine-
dc.titlePRMT1 is the predominant type I protein arginine methyltransferase in mammalian cells.-
dc.typeArticle-
dc.identifier.pmid10713084-
dc.identifier.urlhttp://www.jbc.org/cgi/pmidlookup?view=long&pmid=10713084-
dc.contributor.affiliatedAuthor백, 운기-
dc.type.localJournal Papers-
dc.citation.titleThe Journal of biological chemistry-
dc.citation.volume275-
dc.citation.number11-
dc.citation.date2000-
dc.citation.startPage7723-
dc.citation.endPage7730-
dc.identifier.bibliographicCitationThe Journal of biological chemistry, 275(11). : 7723-7730, 2000-
dc.identifier.eissn1083-351X-
dc.relation.journalidJ000219258-
Appears in Collections:
Journal Papers > School of Medicine / Graduate School of Medicine > Biochemistry & Molecular Biology
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