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首页> 外文期刊>Molecular and Cellular Biology >Cyclic AMP-dependent protein kinase inhibits ADH2 expression in part by decreasing expression of the transcription factor gene ADR1.
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Cyclic AMP-dependent protein kinase inhibits ADH2 expression in part by decreasing expression of the transcription factor gene ADR1.

机译：依赖于环AMP的蛋白激酶部分通过降低转录因子基因ADR1的表达来抑制ADH2的表达。

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In Saccharomyces cerevisiae, the unregulated cyclic AMP-dependent protein kinase (cAPK) activity of bcy1 mutant cells inhibits expression of the glucose-repressible ADH2 gene. The transcription factor Adr1p is thought to be the primary target of cAPK. Here we demonstrate that the decreased abundance of Adr1p in bcy1 mutant cells contributes to the inhibition of ADH2 expression. Activation of ADH2 transcription was blocked in bcy1 mutant cells, and UAS1, the Adr1p binding site in the ADH2 promoter, was sufficient to mediate this effect. Concurrent with this loss of transcriptional activation was an up to 30-fold reduction in the level of Adr1p. Mutating the strong cAPK phosphorylation site at serine 230 did not suppress this effect. Analysis of ADR1 mRNA levels and ADR1-lacZ expression suggested that decreased ADR1 transcription was responsible for the reduced protein level. In contrast to the ADH2 promoter, however, deletion analysis suggested that cAPK does not act through a discrete DNA element in the ADR1 promoter. The amount of Adr1p found in bcy1 mutant cells should have been sufficient to support 23% of the wild-type level of ADH2 expression. Since no ADH2 expression was detectable in bcy1 mutant cells, cAPK must also act by other mechanisms. Overexpression of Adr1p only partially restored ADH2 expression, indicating that some of these mechanisms may impinge upon events at or subsequent to the ADR1-dependent step in ADH2 transcriptional activation.
机译：在酿酒酵母中，bcy1突变细胞的不受调节的环AMP依赖性蛋白激酶（cAPK）活性抑制了葡萄糖可抑制的ADH2基因的表达。转录因子Adr1p被认为是cAPK的主要靶标。在这里，我们证明了bcy1突变细胞中Adr1p丰度的下降有助于抑制ADH2的表达。在bcy1突变细胞中，ADH2转录的激活被阻断，而ADH2启动子中的Adr1p结合位点UAS1足以介导这种作用。与此相关的转录激活损失是Adr1p水平最多降低30倍。突变丝氨酸230处的强cAPK磷酸化位点不会抑制这种作用。对ADR1 mRNA水平和ADR1-lacZ表达的分析表明，减少的ADR1转录是导致蛋白质水平降低的原因。但是，与ADH2启动子相反，缺失分析表明cAPK不能通过ADR1启动子中的离散DNA元件起作用。在bcy1突变细胞中发现的Adr1p数量应足以支持ADH2表达的野生型水平的23％。由于在bcy1突变细胞中未检测到ADH2表达，因此cAPK也必须通过其他机制起作用。 Adr1p的过表达仅部分恢复了ADH2的表达，表明这些机制中的一些可能会影响ADH2转录激活中ADR1依赖性步骤或之后的事件。

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