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.
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机译：精氨酸甲基化在果蝇中的作用尚不清楚。我们通过与哺乳动物精氨酸甲基转移酶的序列同源性鉴定了9个PRMT（蛋白精氨酸甲基转移酶）家族，我们将其命名为DART1至DART9（果蝇精氨酸甲基转移酶1-9）。与哺乳动物PRMT命名法保持一致，DART1，DART4，DART5和DART7是PRMT1，PRMT4，PRMT5和PRMT7的推定同源物。其他DART家族成员与PRMT1相似，但没有可识别的同源物。所有九个基因在果蝇中处于不同的发育阶段。 DART1和DART4对底物（包括组蛋白和RNA结合蛋白）具有精氨酸甲基转移酶活性。甲基化精氨酸残基的氨基酸分析证实DART1和DART4都催化不对称二甲基化精氨酸残基的形成，它们是I型精氨酸甲基转移酶。 D. melanogaster中PRMTs的存在表明果蝇是研究精氨酸甲基化的合适遗传系统。
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