RRC ID 49253
著者 Kimura S, Sawatsubashi S, Ito S, Kouzmenko A, Suzuki E, Zhao Y, Yamagata K, Tanabe M, Ueda T, Fujiyama S, Murata T, Matsukawa H, Takeyama K, Yaegashi N, Kato S.
タイトル Drosophila arginine methyltransferase 1 (DART1) is an ecdysone receptor co-repressor.
ジャーナル Biochem Biophys Res Commun
Abstract Histone arginine methylation is an epigenetic marker that regulates gene expression by defining the chromatin state. Arginine methyltransferases, therefore, serve as transcriptional co-regulators. However, unlike other transcriptional co-regulators, the physiological roles of arginine methyltransferases are poorly understood. Drosophila arginine methyltransferase 1 (DART1), the mammalian PRMT1 homologue, methylates the arginine residue of histone H4 (H4R3me2). Disruption of DART1 in Drosophila by imprecise P-element excision resulted in low viability during metamorphosis in the pupal stages. In the pupal stage, an ecdysone hormone signal is critical for developmental progression. DART1 interacted with the nuclear ecdysone receptor (EcR) in a ligand-dependent manner, and co-repressed EcR in intact flies. These findings suggest that DART1, a histone arginine methyltransferase, is a co-repressor of EcR that is indispensable for normal pupal development in the intact fly.
巻・号 371(4)
ページ 889-93
公開日 2008-7-11
DOI 10.1016/j.bbrc.2008.05.003
PII S0006-291X(08)00899-1
PMID 18468516
MeSH Animals Drosophila Proteins / genetics Drosophila Proteins / metabolism* Drosophila melanogaster / enzymology Drosophila melanogaster / genetics Drosophila melanogaster / growth & development* Genes, Lethal Histones / metabolism Immunoprecipitation Methylation Methyltransferases / genetics Methyltransferases / metabolism* Mutation Receptors, Steroid / metabolism* Repressor Proteins / genetics Repressor Proteins / metabolism*
IF 2.985
引用数 18
WOS 分野 BIOPHYSICS BIOCHEMISTRY & MOLECULAR BIOLOGY
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