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• W2156211472 abstract "Type I protein arginine methyltransferases catalyze the formation of asymmetric ω-N G,N G-dimethylarginine residues by transferring methyl groups fromS-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 glutathioneS-transferase-PRMT1, but not purified FDH, can be cross-linked to the methyl-donor substrateS-adenosyl-l-methionine. We conclude that PRMT1 contributes the major type I protein arginine methyltransferase enzyme activity present in mammalian cells and tissues. Type I protein arginine methyltransferases catalyze the formation of asymmetric ω-N G,N G-dimethylarginine residues by transferring methyl groups fromS-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 glutathioneS-transferase-PRMT1, but not purified FDH, can be cross-linked to the methyl-donor substrateS-adenosyl-l-methionine. We conclude that PRMT1 contributes the major type I protein arginine methyltransferase enzyme activity present in mammalian cells and tissues. protein arginine N-methyltransferase S-adenosyl-l-methionine glutathioneS-transferase fibrillarin glycine-arginine domain fusion protein polyacrylamide gel electrophoresis heterogeneous nuclear ribonucleoprotein 10-formyl-5,6,7,8-tetrahydrofolate 10-formyltetrahydrofolate dehydrogenase adenosine dialdehyde coactivator-associated arginine methyltransferase 1 phosphate-buffered saline S-adenosylhomocysteine Arginine methylation in proteins was discovered over 30 years ago (1.Paik W.K. Kim S. J. Biol. Chem. 1968; 243: 2108-2114Abstract Full Text PDF PubMed Google Scholar, 2.Paik W.K. Kim S. Biochem. Biophys. Res. Commun. 1967; 29: 14-20Crossref PubMed Scopus (115) Google Scholar). At least two types of protein arginineN- methyltransferase (PRMT)1 activities that transfer methyl groups fromS-adenosyl-l-methionine (AdoMet) to the guanidino group of arginine residues exist in mammalian cells (3.Lee H.W. Kim S. Paik W.K. Biochemistry. 1977; 16: 78-85Crossref PubMed Scopus (72) Google Scholar). Type I PRMT enzymes catalyze the formation of ω-monomethylarginine and asymmetric ω-N G,N G-dimethylarginine. Type I substrates include many RNA binding and transporting proteins, transcription factors, nuclear matrix proteins, and cytokines (4.Gary J.D. Clarke S. Prog. Nucleic Acids Res. Mol. Biol. 1998; 61: 65-131Crossref PubMed Google Scholar). Functions of type I arginine methylation in proteins may include regulation of transcription, modulation of the affinity of nucleic acid-binding proteins, regulation of interferon signaling pathways, and targeting of nuclear proteins (4.Gary J.D. Clarke S. Prog. Nucleic Acids Res. Mol. Biol. 1998; 61: 65-131Crossref PubMed Google Scholar, 5.Abramovich C. Yakobson B. Chebath J. Revel M. EMBO J. 1997; 16: 260-266Crossref PubMed Scopus (153) Google Scholar, 6.Altschuler L. Wook J.O. Gurari D. Chebath J. Revel M. J. Interferon Cytokine Res. 1999; 19: 189-195Crossref PubMed Scopus (40) Google Scholar, 7.Pintucci G. Quarto N. Rifkin D.B. Mol. Biol. Cell. 1996; 7: 1249-1258Crossref PubMed Scopus (60) Google Scholar, 8.Shen E.C. Henry M.F. Weiss V.H. Valentini S.R. Silver P.A. Lee M.S. Genes Dev. 1998; 12: 679-691Crossref PubMed Scopus (250) Google Scholar). Type II enzymes catalyze the formation of ω-monomethylarginine and symmetric ω-N G,N′G-dimethylarginine (9.Ghosh S.K. Paik W.K. Kim S. J. Biol. Chem. 1988; 263: 19024-19033Abstract Full Text PDF PubMed Google Scholar, 10.Young P.R. Waickus C.M. Biochem. J. 1988; 250: 221-226Crossref PubMed Scopus (8) Google Scholar). Myelin basic protein is the only known substrate for type II arginine methyltransferase activity (4.Gary J.D. Clarke S. Prog. Nucleic Acids Res. Mol. Biol. 1998; 61: 65-131Crossref PubMed Google Scholar). The type III enzyme, discovered in yeast, catalyzes the monomethylation of the internal δ-guanidino nitrogen atom of arginine residues (11.Zobel-Thropp P. Gary J.D. Clarke S. J. Biol. Chem. 1998; 273: 29283-29286Abstract Full Text Full Text PDF PubMed Scopus (56) Google Scholar).Four enzymatically active type I protein arginineN-methyltransferases have been reported: PRMT1 (12.Lin W.J. Gary J.D. Yang M.C. Clarke S. Herschman H.R. J. Biol. Chem. 1996; 271: 15034-15044Abstract Full Text Full Text PDF PubMed Scopus (389) Google Scholar), PRMT3 (13.Tang J. Gary J.D. Clarke S. Herschman H.R. J. Biol. Chem. 1998; 273: 16935-16945Abstract Full Text Full Text PDF PubMed Scopus (271) Google Scholar), and coactivator-associated arginine methyltransferase 1 (CARM1) (14.Chen D. Ma H. Hong H. Koh S.S. Huang S.M. Schurter B.T. Aswad D.W. Stallcup M.R. Science. 1999; 284: 2174-2177Crossref PubMed Scopus (992) Google Scholar) from mammalian cells and arginine methyltransferase I (RMT1) from yeast (15.Gary J.D. Lin W.J. Yang M.C. Herschman H.R. Clarke S. J. Biol. Chem. 1996; 271: 12585-12594Abstract Full Text Full Text PDF PubMed Scopus (179) Google Scholar). Knockout of RMT1, the only type I PRMT gene in yeast, has no obvious phenotype. However, a mutant allele ofRMT1 is synthetically lethal to yeast in combination with a temperature-sensitive mutant allele of NPL3 (8.Shen E.C. Henry M.F. Weiss V.H. Valentini S.R. Silver P.A. Lee M.S. Genes Dev. 1998; 12: 679-691Crossref PubMed Scopus (250) Google Scholar). NPL3 is an RMT1 substrate involved in nuclear protein import, pre-RNA processing, and export of mRNA from the nucleus (8.Shen E.C. Henry M.F. Weiss V.H. Valentini S.R. Silver P.A. Lee M.S. Genes Dev. 1998; 12: 679-691Crossref PubMed Scopus (250) Google Scholar). PRMT1, the first protein arginine N-methyltransferase in mammalian cells to be cloned, was discovered as a protein interacting with the immediate-early gene products BTG1 and TIS21 (12.Lin W.J. Gary J.D. Yang M.C. Clarke S. Herschman H.R. J. Biol. Chem. 1996; 271: 15034-15044Abstract Full Text Full Text PDF PubMed Scopus (389) Google Scholar). BTG1 and TIS21 are negative regulators of cell growth whose overexpression in cells can lead to cell growth arrest (16.Rouault J.P. Rimokh R. Tessa C. Paranhos G. Ffrench M. Duret L. Garoccio M. Germain D. Samarut J. Magaud J.P. EMBO J. 1992; 11: 1663-1670Crossref PubMed Scopus (266) Google Scholar, 17.Rouault J.P. Falette N. Guehenneux F. Guillot C. Rimokh R. Wang Q. Berthet C. Moyret-Lalle C. Savatier P. Pain B. Shaw P. Berger R. Samarut J. Magaud J.P. Ozturk M. Samarut C. Puisieux A. Nat. Genet. 1996; 14: 482-486Crossref PubMed Scopus (346) Google Scholar). BTG1 and TIS21 interact with PRMT1 and regulate its enzymatic activity (12.Lin W.J. Gary J.D. Yang M.C. Clarke S. Herschman H.R. J. Biol. Chem. 1996; 271: 15034-15044Abstract Full Text Full Text PDF PubMed Scopus (389) Google Scholar). PRMT1 also associates with the interferon α/β receptor (5.Abramovich C. Yakobson B. Chebath J. Revel M. EMBO J. 1997; 16: 260-266Crossref PubMed Scopus (153) Google Scholar, 6.Altschuler L. Wook J.O. Gurari D. Chebath J. Revel M. J. Interferon Cytokine Res. 1999; 19: 189-195Crossref PubMed Scopus (40) Google Scholar). PRMT1, a predominantly nuclear protein, exists in a large complex of 300–400 kDa (12.Lin W.J. Gary J.D. Yang M.C. Clarke S. Herschman H.R. J. Biol. Chem. 1996; 271: 15034-15044Abstract Full Text Full Text PDF PubMed Scopus (389) Google Scholar, 13.Tang J. Gary J.D. Clarke S. Herschman H.R. J. Biol. Chem. 1998; 273: 16935-16945Abstract Full Text Full Text PDF PubMed Scopus (271) Google Scholar) and methylates arginine residues in RGG and RXR motifs of many RNA-binding proteins and other proteins (4.Gary J.D. Clarke S. Prog. Nucleic Acids Res. Mol. Biol. 1998; 61: 65-131Crossref PubMed Google Scholar, 18.Smith J.J. Rucknagel K.P. Schierhorn A. Tang J. Nemeth A. Linder M. Herschman H.R. Wahle E. J. Biol. Chem. 1999; 274: 13229-13234Abstract Full Text Full Text PDF PubMed Scopus (135) Google Scholar). PRMT2 was identified because of its sequence similarity to PRMT1 (19.Scott H.S. Antonarakis S.E. Lalioti M.D. Rossier C. Silver P.A. Henry M.F. Genomics. 1998; 48: 330-340Crossref PubMed Scopus (143) Google Scholar). To date no methyltransferase activity has been demonstrated for PRMT2. PRMT3 is a monomeric cytoplasmic protein whose activity overlaps with that of PRMT1 (13.Tang J. Gary J.D. Clarke S. Herschman H.R. J. Biol. Chem. 1998; 273: 16935-16945Abstract Full Text Full Text PDF PubMed Scopus (271) Google Scholar). CARM1, the third active mammalian arginine methyltransferase to be discovered, was cloned as a protein interacting with the carboxyl-terminal region of p160 coactivator (14.Chen D. Ma H. Hong H. Koh S.S. Huang S.M. Schurter B.T. Aswad D.W. Stallcup M.R. Science. 1999; 284: 2174-2177Crossref PubMed Scopus (992) Google Scholar). PRMT1, PRMT2, PRMT3, CARM1, and yeast RMT1 all contain signature regions (I, post-I, -II, and -III) that constitute the core of the AdoMet-binding site (20.Kagan R.M. Clarke S. Arch. Biochem. Biophys. 1994; 310: 417-427Crossref PubMed Scopus (419) Google Scholar).In a recent study, the predominant protein arginineN-methyltransferase was purified from rat liver (21.Kim S. Park G.H. Joo W.A. Paik W.K. Cook R.J. Williams K.R. J. Biol. Chem. 1998; 273: 27374-27382Abstract Full Text Full Text PDF PubMed Scopus (5) Google Scholar). Sequence analysis identified the major polypeptide in this preparation as 10-formyltetrahydrofolate dehydrogenase (FDH, EC 1.5.1.6), suggesting that the major protein arginine methyltransferase may be encoded by a gene encoding an enzyme involved in folate metabolism. FDH catalyzes (i) NADP+-dependent oxidation of 10-formyltetrahydrofolate (10-FTHF) to tetrahydrofolate, NADPH, and CO2; (ii) NADP+-independent hydrolysis of 10-FTHF to formate and tetrahydrofolate; and (iii) NADP+-dependent oxidation of 2-propanal (22.Cook R.J. Lloyd R.S. Wagner C. J. Biol. Chem. 1991; 266: 4965-4973Abstract Full Text PDF PubMed Google Scholar,23.Cook R.J. Wagner C. Arch. Biochem. Biophys. 1995; 321: 336-344Crossref PubMed Scopus (13) Google Scholar). FDH purified from rat liver exists as a tetramer of identical 99-kDa subunits (22.Cook R.J. Lloyd R.S. Wagner C. J. Biol. Chem. 1991; 266: 4965-4973Abstract Full Text PDF PubMed Google Scholar, 24.Scrutton M.C. Beis I. Biochem. J. 1979; 177: 833-846Crossref PubMed Scopus (28) Google Scholar, 25.Min H. Shane B. Stokstad E.L. Biochim. Biophys. Acta. 1988; 967: 348-353Crossref PubMed Scopus (49) Google Scholar). The cDNA-deduced FDH amino acid sequence contains several domains (22.Cook R.J. Lloyd R.S. Wagner C. J. Biol. Chem. 1991; 266: 4965-4973Abstract Full Text PDF PubMed Google Scholar, 26.Schirch D. Villar E. Maras B. Barra D. Schirch V. J. Biol. Chem. 1994; 269: 24728-24735Abstract Full Text PDF PubMed Google Scholar), including the amino-terminal phosphoribosyl-glycinamide formyltransferase homologous domain (amino acids 1–203) (27.Krupenko S.A. Wagner C. Cook R.J. J. Biol. Chem. 1997; 272: 10273-10278Abstract Full Text Full Text PDF PubMed Scopus (31) Google Scholar) and the carboxyl-terminal aldehyde dehydrogenase homologous domain (amino acids 417–902) (28.Krupenko S.A. Wagner C. Cook R.J. J. Biol. Chem. 1997; 272: 10266-10272Abstract Full Text Full Text PDF PubMed Scopus (45) Google Scholar). However, FDH does not contain any methyltransferase signature sequences (20.Kagan R.M. Clarke S. Arch. Biochem. Biophys. 1994; 310: 417-427Crossref PubMed Scopus (419) Google Scholar).To understand further the relationship between the PRMT and FDH gene products, we sought to identify the major type I protein arginineN-methyltransferase in cells and tissues. We used cultured rat cells and tissues from FDH(+/+), FDH(+/−), and FDH(−/−) mice to determine (i) which methyltransferase is the predominant type I protein arginine methyltransferase and (ii) whether the protein arginine methyltransferase activity in FDH enzyme preparations is catalyzed by the FDH enzyme or by a copurified, but distinct, methyltransferase. Arginine methylation in proteins was discovered over 30 years ago (1.Paik W.K. Kim S. J. Biol. Chem. 1968; 243: 2108-2114Abstract Full Text PDF PubMed Google Scholar, 2.Paik W.K. Kim S. Biochem. Biophys. Res. Commun. 1967; 29: 14-20Crossref PubMed Scopus (115) Google Scholar). At least two types of protein arginineN- methyltransferase (PRMT)1 activities that transfer methyl groups fromS-adenosyl-l-methionine (AdoMet) to the guanidino group of arginine residues exist in mammalian cells (3.Lee H.W. Kim S. Paik W.K. Biochemistry. 1977; 16: 78-85Crossref PubMed Scopus (72) Google Scholar). Type I PRMT enzymes catalyze the formation of ω-monomethylarginine and asymmetric ω-N G,N G-dimethylarginine. Type I substrates include many RNA binding and transporting proteins, transcription factors, nuclear matrix proteins, and cytokines (4.Gary J.D. Clarke S. Prog. Nucleic Acids Res. Mol. Biol. 1998; 61: 65-131Crossref PubMed Google Scholar). Functions of type I arginine methylation in proteins may include regulation of transcription, modulation of the affinity of nucleic acid-binding proteins, regulation of interferon signaling pathways, and targeting of nuclear proteins (4.Gary J.D. Clarke S. Prog. Nucleic Acids Res. Mol. Biol. 1998; 61: 65-131Crossref PubMed Google Scholar, 5.Abramovich C. Yakobson B. Chebath J. Revel M. EMBO J. 1997; 16: 260-266Crossref PubMed Scopus (153) Google Scholar, 6.Altschuler L. Wook J.O. Gurari D. Chebath J. Revel M. J. Interferon Cytokine Res. 1999; 19: 189-195Crossref PubMed Scopus (40) Google Scholar, 7.Pintucci G. Quarto N. Rifkin D.B. Mol. Biol. Cell. 1996; 7: 1249-1258Crossref PubMed Scopus (60) Google Scholar, 8.Shen E.C. Henry M.F. Weiss V.H. Valentini S.R. Silver P.A. Lee M.S. Genes Dev. 1998; 12: 679-691Crossref PubMed Scopus (250) Google Scholar). Type II enzymes catalyze the formation of ω-monomethylarginine and symmetric ω-N G,N′G-dimethylarginine (9.Ghosh S.K. Paik W.K. Kim S. J. Biol. Chem. 1988; 263: 19024-19033Abstract Full Text PDF PubMed Google Scholar, 10.Young P.R. Waickus C.M. Biochem. J. 1988; 250: 221-226Crossref PubMed Scopus (8) Google Scholar). Myelin basic protein is the only known substrate for type II arginine methyltransferase activity (4.Gary J.D. Clarke S. Prog. Nucleic Acids Res. Mol. Biol. 1998; 61: 65-131Crossref PubMed Google Scholar). The type III enzyme, discovered in yeast, catalyzes the monomethylation of the internal δ-guanidino nitrogen atom of arginine residues (11.Zobel-Thropp P. Gary J.D. Clarke S. J. Biol. Chem. 1998; 273: 29283-29286Abstract Full Text Full Text PDF PubMed Scopus (56) Google Scholar). Four enzymatically active type I protein arginineN-methyltransferases have been reported: PRMT1 (12.Lin W.J. Gary J.D. Yang M.C. Clarke S. Herschman H.R. J. Biol. Chem. 1996; 271: 15034-15044Abstract Full Text Full Text PDF PubMed Scopus (389) Google Scholar), PRMT3 (13.Tang J. Gary J.D. Clarke S. Herschman H.R. J. Biol. Chem. 1998; 273: 16935-16945Abstract Full Text Full Text PDF PubMed Scopus (271) Google Scholar), and coactivator-associated arginine methyltransferase 1 (CARM1) (14.Chen D. Ma H. Hong H. Koh S.S. Huang S.M. Schurter B.T. Aswad D.W. Stallcup M.R. Science. 1999; 284: 2174-2177Crossref PubMed Scopus (992) Google Scholar) from mammalian cells and arginine methyltransferase I (RMT1) from yeast (15.Gary J.D. Lin W.J. Yang M.C. Herschman H.R. Clarke S. J. Biol. Chem. 1996; 271: 12585-12594Abstract Full Text Full Text PDF PubMed Scopus (179) Google Scholar). Knockout of RMT1, the only type I PRMT gene in yeast, has no obvious phenotype. However, a mutant allele ofRMT1 is synthetically lethal to yeast in combination with a temperature-sensitive mutant allele of NPL3 (8.Shen E.C. Henry M.F. Weiss V.H. Valentini S.R. Silver P.A. Lee M.S. Genes Dev. 1998; 12: 679-691Crossref PubMed Scopus (250) Google Scholar). NPL3 is an RMT1 substrate involved in nuclear protein import, pre-RNA processing, and export of mRNA from the nucleus (8.Shen E.C. Henry M.F. Weiss V.H. Valentini S.R. Silver P.A. Lee M.S. Genes Dev. 1998; 12: 679-691Crossref PubMed Scopus (250) Google Scholar). PRMT1, the first protein arginine N-methyltransferase in mammalian cells to be cloned, was discovered as a protein interacting with the immediate-early gene products BTG1 and TIS21 (12.Lin W.J. Gary J.D. Yang M.C. Clarke S. Herschman H.R. J. Biol. Chem. 1996; 271: 15034-15044Abstract Full Text Full Text PDF PubMed Scopus (389) Google Scholar). BTG1 and TIS21 are negative regulators of cell growth whose overexpression in cells can lead to cell growth arrest (16.Rouault J.P. Rimokh R. Tessa C. Paranhos G. Ffrench M. Duret L. Garoccio M. Germain D. Samarut J. Magaud J.P. EMBO J. 1992; 11: 1663-1670Crossref PubMed Scopus (266) Google Scholar, 17.Rouault J.P. Falette N. Guehenneux F. Guillot C. Rimokh R. Wang Q. Berthet C. Moyret-Lalle C. Savatier P. Pain B. Shaw P. Berger R. Samarut J. Magaud J.P. Ozturk M. Samarut C. Puisieux A. Nat. Genet. 1996; 14: 482-486Crossref PubMed Scopus (346) Google Scholar). BTG1 and TIS21 interact with PRMT1 and regulate its enzymatic activity (12.Lin W.J. Gary J.D. Yang M.C. Clarke S. Herschman H.R. J. Biol. Chem. 1996; 271: 15034-15044Abstract Full Text Full Text PDF PubMed Scopus (389) Google Scholar). PRMT1 also associates with the interferon α/β receptor (5.Abramovich C. Yakobson B. Chebath J. Revel M. EMBO J. 1997; 16: 260-266Crossref PubMed Scopus (153) Google Scholar, 6.Altschuler L. Wook J.O. Gurari D. Chebath J. Revel M. J. Interferon Cytokine Res. 1999; 19: 189-195Crossref PubMed Scopus (40) Google Scholar). PRMT1, a predominantly nuclear protein, exists in a large complex of 300–400 kDa (12.Lin W.J. Gary J.D. Yang M.C. Clarke S. Herschman H.R. J. Biol. Chem. 1996; 271: 15034-15044Abstract Full Text Full Text PDF PubMed Scopus (389) Google Scholar, 13.Tang J. Gary J.D. Clarke S. Herschman H.R. J. Biol. Chem. 1998; 273: 16935-16945Abstract Full Text Full Text PDF PubMed Scopus (271) Google Scholar) and methylates arginine residues in RGG and RXR motifs of many RNA-binding proteins and other proteins (4.Gary J.D. Clarke S. Prog. Nucleic Acids Res. Mol. Biol. 1998; 61: 65-131Crossref PubMed Google Scholar, 18.Smith J.J. Rucknagel K.P. Schierhorn A. Tang J. Nemeth A. Linder M. Herschman H.R. Wahle E. J. Biol. Chem. 1999; 274: 13229-13234Abstract Full Text Full Text PDF PubMed Scopus (135) Google Scholar). PRMT2 was identified because of its sequence similarity to PRMT1 (19.Scott H.S. Antonarakis S.E. Lalioti M.D. Rossier C. Silver P.A. Henry M.F. Genomics. 1998; 48: 330-340Crossref PubMed Scopus (143) Google Scholar). To date no methyltransferase activity has been demonstrated for PRMT2. PRMT3 is a monomeric cytoplasmic protein whose activity overlaps with that of PRMT1 (13.Tang J. Gary J.D. Clarke S. Herschman H.R. J. Biol. Chem. 1998; 273: 16935-16945Abstract Full Text Full Text PDF PubMed Scopus (271) Google Scholar). CARM1, the third active mammalian arginine methyltransferase to be discovered, was cloned as a protein interacting with the carboxyl-terminal region of p160 coactivator (14.Chen D. Ma H. Hong H. Koh S.S. Huang S.M. Schurter B.T. Aswad D.W. Stallcup M.R. Science. 1999; 284: 2174-2177Crossref PubMed Scopus (992) Google Scholar). PRMT1, PRMT2, PRMT3, CARM1, and yeast RMT1 all contain signature regions (I, post-I, -II, and -III) that constitute the core of the AdoMet-binding site (20.Kagan R.M. Clarke S. Arch. Biochem. Biophys. 1994; 310: 417-427Crossref PubMed Scopus (419) Google Scholar). In a recent study, the predominant protein arginineN-methyltransferase was purified from rat liver (21.Kim S. Park G.H. Joo W.A. Paik W.K. Cook R.J. Williams K.R. J. Biol. Chem. 1998; 273: 27374-27382Abstract Full Text Full Text PDF PubMed Scopus (5) Google Scholar). Sequence analysis identified the major polypeptide in this preparation as 10-formyltetrahydrofolate dehydrogenase (FDH, EC 1.5.1.6), suggesting that the major protein arginine methyltransferase may be encoded by a gene encoding an enzyme involved in folate metabolism. FDH catalyzes (i) NADP+-dependent oxidation of 10-formyltetrahydrofolate (10-FTHF) to tetrahydrofolate, NADPH, and CO2; (ii) NADP+-independent hydrolysis of 10-FTHF to formate and tetrahydrofolate; and (iii) NADP+-dependent oxidation of 2-propanal (22.Cook R.J. Lloyd R.S. Wagner C. J. Biol. Chem. 1991; 266: 4965-4973Abstract Full Text PDF PubMed Google Scholar,23.Cook R.J. Wagner C. Arch. Biochem. Biophys. 1995; 321: 336-344Crossref PubMed Scopus (13) Google Scholar). FDH purified from rat liver exists as a tetramer of identical 99-kDa subunits (22.Cook R.J. Lloyd R.S. Wagner C. J. Biol. Chem. 1991; 266: 4965-4973Abstract Full Text PDF PubMed Google Scholar, 24.Scrutton M.C. Beis I. Biochem. J. 1979; 177: 833-846Crossref PubMed Scopus (28) Google Scholar, 25.Min H. Shane B. Stokstad E.L. Biochim. Biophys. Acta. 1988; 967: 348-353Crossref PubMed Scopus (49) Google Scholar). The cDNA-deduced FDH amino acid sequence contains several domains (22.Cook R.J. Lloyd R.S. Wagner C. J. Biol. Chem. 1991; 266: 4965-4973Abstract Full Text PDF PubMed Google Scholar, 26.Schirch D. Villar E. Maras B. Barra D. Schirch V. J. Biol. Chem. 1994; 269: 24728-24735Abstract Full Text PDF PubMed Google Scholar), including the amino-terminal phosphoribosyl-glycinamide formyltransferase homologous domain (amino acids 1–203) (27.Krupenko S.A. Wagner C. Cook R.J. J. Biol. Chem. 1997; 272: 10273-10278Abstract Full Text Full Text PDF PubMed Scopus (31) Google Scholar) and the carboxyl-terminal aldehyde dehydrogenase homologous domain (amino acids 417–902) (28.Krupenko S.A. Wagner C. Cook R.J. J. Biol. Chem. 1997; 272: 10266-10272Abstract Full Text Full Text PDF PubMed Scopus (45) Google Scholar). However, FDH does not contain any methyltransferase signature sequences (20.Kagan R.M. Clarke S. Arch. Biochem. Biophys. 1994; 310: 417-427Crossref PubMed Scopus (419) Google Scholar). To understand further the relationship between the PRMT and FDH gene products, we sought to identify the major type I protein arginineN-methyltransferase in cells and tissues. We used cultured rat cells and tissues from FDH(+/+), FDH(+/−), and FDH(−/−) mice to determine (i) which methyltransferase is the predominant type I protein arginine methyltransferase and (ii) whether the protein arginine methyltransferase activity in FDH enzyme preparations is catalyzed by the FDH enzyme or by a copurified, but distinct, methyltransferase. We thank the members of the Herschman and Clarke labs for helpful discussions. We also thank Rick B. Dye (Vanderbilt University School of Medicine) for raising the FDH-deficient mice and purifying rat liver FDH." @default.
• W2156211472 created "2016-06-24" @default.
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• W2156211472 date "2000-03-01" @default.
• W2156211472 modified "2023-10-18" @default.
• W2156211472 title "PRMT1 Is the Predominant Type I Protein Arginine Methyltransferase in Mammalian Cells" @default.
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