PMID:14705965

Citation	Boulanger, MC, Miranda, TB, Clarke, S, Di Fruscio, M, Suter, B, Lasko, P and Richard, S (2004) Characterization of the Drosophila protein arginine methyltransferases DART1 and DART4. Biochem. J. 379:283-9
Abstract	The role of arginine methylation in Drosophila melanogaster is unknown. We identified a family of nine PRMTs (protein arginine methyltransferases) by sequence homology with mammalian arginine methyltransferases, which we have named DART1 to DART9 ( Drosophila arginine methyltransferases 1-9). In keeping with the mammalian PRMT nomenclature, DART1, DART4, DART5 and DART7 are the putative homologues of PRMT1, PRMT4, PRMT5 and PRMT7. Other DART family members have a closer resemblance to PRMT1, but do not have identifiable homologues. All nine genes are expressed in Drosophila at various developmental stages. DART1 and DART4 have arginine methyltransferase activity towards substrates, including histones and RNA-binding proteins. Amino acid analysis of the methylated arginine residues confirmed that both DART1 and DART4 catalyse the formation of asymmetrical dimethylated arginine residues and they are type I arginine methyltransferases. The presence of PRMTs in D. melanogaster suggest that flies are a suitable genetic system to study arginine methylation.
Links	PubMed PMC1224071 Online version:10.1042/BJ20031176
Keywords	Amino Acid Sequence; Animals; Drosophila Proteins/genetics; Drosophila Proteins/metabolism; Drosophila melanogaster/embryology; Drosophila melanogaster/enzymology; Drosophila melanogaster/growth & development; Female; Male; Methyltransferases/genetics; Methyltransferases/metabolism; Molecular Sequence Data; Protein-Arginine N-Methyltransferases/genetics; Protein-Arginine N-Methyltransferases/metabolism; RNA, Messenger/metabolism; Sequence Homology, Amino Acid
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