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首页> 外文期刊>Nucleic acids research >The Drosophila engrailed protein is phosphorylated by a serine-specific protein kinase
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The Drosophila engrailed protein is phosphorylated by a serine-specific protein kinase

机译:果蝇吞噬的蛋白被丝氨酸特异性蛋白激酶磷酸化。

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The engrailed gene is required during embryogenesis of Drosophila melanogaster for normal segmental development and for differentiation of posterior compartments. The protein encoded by the engrailed gene contains a homeodomain, has sequence specific DNA binding activity, and has been proposed as a transcriptional regulator. We show here that the engrailed protein, isolated from both cultured cells and embryos, has been modified by a serine-specific protein kinase. This is the first report that homeobox proteins are post-translationally modified. Phosphorylation of the engrailed protein may directly or allosterically modify its function, and offers the possibility that the engrailed protein becomes phosphorylated in response to extracellular, mitogenic or positional stimuli.
机译:在正常果蝇的发育和后房的分化过程中,果蝇的胚胎发生过程中需要该基因。由融合基因编码的蛋白质包含一个同源结构域,具有序列特异性的DNA结合活性,并被提议作为转录调节因子。我们在这里表明,从培养的细胞和胚胎中分离出的蛋白质,已经被丝氨酸特异性蛋白激酶修饰。这是关于同源异型盒蛋白质被翻译后修饰的第一份报道。突入蛋白质的磷酸化可以直接或变构改变其功能,并提供了突入蛋白质响应于细胞外,促有丝分裂或位置刺激而被磷酸化的可能性。

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