RRC ID |
49253
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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.
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タイトル |
Drosophila arginine methyltransferase 1 (DART1) is an ecdysone receptor co-repressor.
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ジャーナル |
Biochem Biophys Res Commun
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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.
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巻・号 |
371(4)
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ページ |
889-93
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公開日 |
2008-7-11
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DOI |
10.1016/j.bbrc.2008.05.003
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PII |
S0006-291X(08)00899-1
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PMID |
18468516
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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
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引用数 |
18
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WOS 分野
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BIOPHYSICS
BIOCHEMISTRY & MOLECULAR BIOLOGY
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リソース情報 |
ショウジョウバエ |
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