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首页> 外文期刊>Molecular and Cellular Biology >Yeast SNF1 protein kinase interacts with SIP4, a C6 zinc cluster transcriptional activator: a new role for SNF1 in the glucose response.
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Yeast SNF1 protein kinase interacts with SIP4, a C6 zinc cluster transcriptional activator: a new role for SNF1 in the glucose response.

机译：酵母SNF1蛋白激酶与C6锌簇转录激活因子SIP4相互作用：SNF1在葡萄糖反应中的新作用。

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摘要

The SNF1 protein kinase has been widely conserved in plants and mammals. In Saccharomyces cerevisiae, SNF1 is essential for expression of glucose-repressed genes in response to glucose deprivation. Previous studies supported a role for SNF1 in relieving transcriptional repression. Here, we report evidence that SNF1 modulates function of a transcriptional activator, SIP4, which was identified in a two-hybrid screen for interaction with SNF1. The N terminus of the predicted 96-kDa SIP4 protein is homologous to the DNA-binding domain of the GAL4 family of transcriptional activators, with a C6 zinc cluster adjacent to a coiled-coil motif The C terminus contains a leucine zipper motif and an acidic region. When bound to DNA, a LexA-SIP4 fusion activates transcription of a reporter gene. Transcriptional activation by SIP4 is regulated by glucose and depends on the SNF1 protein kinase. Moreover, SIP4 is differentially phosphorylated in response to glucose availability, and phosphorylation requires SNF1. These findings suggest that the SNF1 kinase interacts with a transcriptional activator to modulate its activity and provide the first direct evidence for a role of SNF1 in activating transcription in response to glucose limitation.
机译：SNF1蛋白激酶已在植物和哺乳动物中广泛保存。在酿酒酵母中，SNF1对于响应葡萄糖剥夺的葡萄糖抑制基因的表达至关重要。先前的研究支持SNF1在减轻转录抑制中的作用。在这里，我们报告的证据表明SNF1调节转录激活因子SIP4的功能，该转录激活因子在与SNF1相互作用的双重杂交筛选中被确定。预测的96 kDa SIP4蛋白的N末端与转录激活因子GAL4家族的DNA结合结构域同源，C6锌簇与卷曲螺旋基序相邻。C末端包含亮氨酸拉链基序和酸性地区。当与DNA结合时，LexA-SIP4融合体会激活报告基因的转录。 SIP4的转录激活受葡萄糖调节，并取决于SNF1蛋白激酶。此外，SIP4响应葡萄糖的可用性而被差异磷酸化，磷酸化需要SNF1。这些发现表明，SNF1激酶与转录激活因子相互作用以调节其活性，并为SNF1在响应葡萄糖限制而激活转录中的作用提供了第一个直接证据。

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