title: Arginine methylation of scaffold attachment factor A by heterogeneous nuclear ribonucleoprotein particle-associated PRMT1.
abstract: Components of the heterogeneous nuclear ribonucleoprotein (hnRNP) complex and other nucleic acid-binding proteins are subject to methylation on specific arginine residues by the catalytic activity of arginine methyltransferases. The methylation has been implicated in transcriptional regulation and RNA and protein trafficking and signal transduction, but the mechanism by which these functions are achieved has remained undetermined. We show here that the predominant arginine methyltransferase in human cells, protein arginine methyltransferase 1 (PRMT1), is associated with hnRNP complexes, dependent on the methylation status of the cell, and that it methylates its preferred substrates in situ. Binding of PRMT1 occurs through physical interaction with scaffold attachment factor A (SAF-A), also known as hnRNP-U, which is quantitatively methylated by PRMT1 in all investigated cell lines as determined by a novel, highly specific, methylation-sensitive antibody.
authors.affiliation: Department of Molecular Cell Biology, Heinrich-Pette-Institute, Martinistrasse 52, 20251 Hamburg, Germany.
authors.forename: Frank
authors.initials: F
authors.lastname: Herrmann
authors.forename: Maike
authors.initials: M
authors.lastname: Bossert
authors.forename: Andrea
authors.initials: A
authors.lastname: Schwander
authors.forename: Ercan
authors.initials: E
authors.lastname: Akgün
authors.forename: Frank O
authors.initials: FO
authors.lastname: Fackelmayer
mesh_terms: D000818:Animals; D001120:Arginine / Q000737:chemistry*; D015153:Blotting, Western; D002460:Cell Line; D002499:Centrifugation, Density Gradient; D019175:DNA Methylation; D004591:Electrophoresis, Polyacrylamide Gel; D005982:Glutathione Transferase / Q000378:metabolism; D005990:Glycerol / Q000737:chemistry; D034722:Heterogeneous-Nuclear Ribonucleoprotein U / Q000737:chemistry* / Q000378:metabolism; D034441:Heterogeneous-Nuclear Ribonucleoproteins / Q000378:metabolism*; D006801:Humans; D047468:Immunoprecipitation; D008745:Methylation; D008856:Microscopy, Fluorescence; D011485:Protein Binding; D011484:Protein-Arginine N-Methyltransferases / Q000235:genetics / Q000378:metabolism*; D012313:RNA / Q000378:metabolism; D011994:Recombinant Proteins / Q000737:chemistry; D015398:Signal Transduction; D014158:Transcription, Genetic; D014162:Transfection
chemical_list: D034722:Heterogeneous-Nuclear Ribonucleoprotein U; D034441:Heterogeneous-Nuclear Ribonucleoproteins; D011994:Recombinant Proteins; D012313:RNA; D001120:Arginine; D011484:Protein-Arginine N-Methyltransferases; C464934:protein arginine methyltransferase 2; D005982:Glutathione Transferase; D005990:Glycerol