title: Unusual sites of arginine methylation in Poly(A)-binding protein II and in vitro methylation by protein arginine methyltransferases PRMT1 and PRMT3.
abstract: Arginine methylation is a post-translational modification found mostly in RNA-binding proteins. Poly(A)-binding protein II from calf thymus was shown by mass spectrometry and sequencing to contain NG, NG-dimethylarginine at 13 positions in its amino acid sequence. Two additional arginine residues were partially methylated. Almost all of the modified residues were found in Arg-Xaa-Arg clusters in the C terminus of the protein. These motifs are distinct from Arg-Gly-Gly motifs that have been previously described as sites and specificity determinants for asymmetric arginine dimethylation. Poly(A)-binding protein II and deletion mutants expressed in Escherichia coli were in vitro substrates for two mammalian protein arginine methyltransferases, PRMT1 and PRMT3, with S-adenosyl-L-methionine as the methyl group donor. Both PRMT1 and PRMT3 specifically methylated arginines in the C-terminal domain corresponding to the naturally modified sites.
authors.affiliation: Institut für Biochemie, Martin-Luther-Universität Halle-Wittenberg, 06120 Halle, Germany.
authors.forename: J J
authors.initials: JJ
authors.lastname: Smith
authors.forename: K P
authors.initials: KP
authors.lastname: Rücknagel
authors.forename: A
authors.initials: A
authors.lastname: Schierhorn
authors.forename: J
authors.initials: J
authors.lastname: Tang
authors.forename: A
authors.initials: A
authors.lastname: Nemeth
authors.forename: M
authors.initials: M
authors.lastname: Linder
authors.forename: H R
authors.initials: HR
authors.lastname: Herschman
authors.forename: E
authors.initials: E
authors.lastname: Wahle
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001120:Arginine / Q000378:metabolism*; D002417:Cattle; D018076:DNA, Complementary; D007527:Isoenzymes / Q000235:genetics / Q000378:metabolism*; D008745:Methylation; D008969:Molecular Sequence Data; D039102:Poly(A)-Binding Proteins; D011484:Protein-Arginine N-Methyltransferases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D016601:RNA-Binding Proteins / Q000378:metabolism*; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D017384:Sequence Deletion; D013379:Substrate Specificity; D013950:Thymus Gland / Q000378:metabolism
chemical_list: D018076:DNA, Complementary; D007527:Isoenzymes; D039102:Poly(A)-Binding Proteins; D016601:RNA-Binding Proteins; D011994:Recombinant Proteins; D001120:Arginine; D011484:Protein-Arginine N-Methyltransferases