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首页> 外文期刊>Molecular and Cellular Biology >Key Role of Ser562/661 in Snf1-Dependent Regulation of Cat8p in Saccharomyces cerevisiae and Kluyveromyces lactis
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Key Role of Ser562/661 in Snf1-Dependent Regulation of Cat8p in Saccharomyces cerevisiae and Kluyveromyces lactis

机译：Ser562 / 661在酿酒酵母和乳酸克鲁维酵母中Cat8p的Snf1依赖性调节中的关键作用。

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Utilization of nonfermentable carbon sources by Kluyveromyces lactis and Saccharomyces cerevisiae requires the Snf1p kinase and the Cat8p transcriptional activator, which binds to carbon source-responsive elements of target genes. We demonstrate that KlSnf1p and KlCat8p from K. lactis interact in a two-hybrid system and that the interaction is stronger with a kinase-dead mutant form of KlSnf1p. Of two putative phosphorylation sites in the KlCat8p sequence, serine 661 was identified as a key residue governing KlCat8p regulation. Serine 661 is located in the middle homology region, a regulatory domain conserved among zinc cluster transcription factors, and is part of an Snf1p consensus phosphorylation site. Single mutations at this site are sufficient to completely change the carbon source regulation of the KlCat8p transactivation activity observed. A serine-to-glutamate mutant form mimicking constitutive phosphorylation results in a nearly constitutively active form of KlCat8p, while a serine-to-alanine mutation has the reverse effect. Furthermore, it is shown that KlCat8p phosphorylation depends on KlSNF1. The Snf1-Cat8 connection is evolutionarily conserved: mutation of corresponding serine 562 of ScCat8p gave similar results in S. cerevisiae. The enhanced capacity of ScCat8S562E to suppress the phenotype caused by snf1 strengthens the hypothesis of direct phosphorylation of Cat8p by Snf1p. Unlike that of S. cerevisiae ScCAT8, KlCAT8 transcription is not carbon source regulated, illustrating the prominent role of posttranscriptional regulation of Cat8p in K. lactis.
机译：乳酸克鲁维酵母和酿酒酵母利用不可发酵的碳源需要Snf1p激酶和Cat8p转录激活因子，它们与靶基因的碳源响应元件结合。我们证明了 K的KlSnf1p和KlCat8p。乳酸在两个杂交系统中相互作用，并且与激酶死亡的突变型KlSnf1p相互作用更强。在K1Cat8p序列中的两个推定的磷酸化位点中，丝氨酸661被鉴定为控制K1Cat8p调节的关键残基。丝氨酸661位于中间同源区域，在锌簇转录因子之间保守的调节域，并且是Snf1p共有磷酸化位点的一部分。在该位点的单个突变足以完全改变所观察到的KlCat8p反式激活活性的碳源调节。模仿组成型磷酸化的丝氨酸到谷氨酸突变体形式导致了KlCat8p的几乎组成性活性形式，而丝氨酸到丙氨酸突变具有相反的作用。此外，还表明KlCat8p的磷酸化取决于 KlSNF1 。 Snf1-Cat8连接在进化上是保守的：ScCat8p相应丝氨酸562的突变在 S中给出了相似的结果。啤酒酵母。 ScCat8S562E抑制由 snf1 引起的表型的能力增强，这增强了Snf1p对Cat8p直接磷酸化的假设。与 S不同。酿酒酵母ScCAT8 ， KlCAT8 的转录不受碳源调控，这说明了Cat8p转录后调控在 K中的重要作用。乳酸。

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