ヒロタ　ケイコ   Keiko HIROTA   廣田　恵子    所属   医学部 医学科    職種   講師
論文種別	原著
言語種別	英語
査読の有無	査読あり
表題	PRMT-5 converts monomethylarginines into symmetrical dimethylarginines in Caenorhabditis elegans.
掲載誌名	正式名：The Journal of Biochemistry ISSNコード：0021924X
掲載区分	国外
巻・号・頁	161(1),pp.231-235
著者・共著者	KANOU Akihiko†, KAKO Koichiro, HIROTA Keiko, FUKAMIZU Akiyoshi*
発行年月	2017/02
概要	The transmethylation to arginine residues of proteins is catalyzed by protein arginine methyltransferases (PRMTs) that form monomethylarginine (MMA), asymmetric (ADMA) and symmetric dimethylarginines (SDMA). Although we previously demonstrated that the generation of ADMA residues in whole proteins is driven by PRMT-1 in Caenorhabditis elegans, much less is known about MMA and SDMA in vivo. In this study, we measured the amounts of different methylarginines in whole protein extracts made from wild-type (N2) C. elegans and from prmt-1 and prmt-5 null mutants using liquid chromatography-tandem mass spectrometry. Interestingly, we found that the amounts of MMA and SDMA are about fourfold higher than those of ADMA in N2 protein lysates using acid hydrolysis. We were unable to detect SDMA residues in the prmt-5 null mutant. In comparison with N2, an increase in SDMA and decrease in MMA were observed in prmt-1 mutant worms with no ADMA, but ADMA and MMA levels were unchanged in prmt-5 mutant worms. These results suggest that PRMT-1 contributes, at least in part, to MMA production, but that PRMT-5 catalyzes the symmetric dimethylation of substrates containing MMA residues in vivo.
DOI	10.1093/jb/mvw066.