Biochemical Journal

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Research article

Characterization of the Drosophila protein arginine methyltransferases DART1 and DART4

Marie-Chloé BOULANGER, Tina Branscombe MIRANDA, Steven CLARKE, Marco di FRUSCIO, Beat SUTER, Paul LASKO, Stéphane RICHARD


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 (Drosophilaarginine 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.

  • arginine methylation
  • cell cycle
  • Drosophila
  • methyltransferase


  • The nucleotide sequences for DART1 to DART9 have been deposited in the GenBank® Nucleotide Sequence Database under the accession numbers AE003688, AE003577, AE003708, AE003685, AE003807, AE003702, AE003459, AE003630, AE003702.

  • Abbreviations used: ADMA, asymmetrical ω-NG,NG-dimethylated arginine residue; CARM1, co-activator-associated arginine methyltransferase 1; DART, Drosophilaarginine methyltransferase; GST, glutathione S-transferase; MBP, myelin basic protein; ω-MMA, ω-monomethylarginine; PABP, poly(A)+-binding protein; PRMT, protein arginine methyltransferase; SDMA, symmetrical ω-NG,NG´-dimethylated arginine residue.