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首页> 外文期刊>Molecular and Cellular Biology >Suppression of a yeast cyclic AMP-dependent protein kinase defect by overexpression of SOK1, a yeast gene exhibiting sequence similarity to a developmentally regulated mouse gene.
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Suppression of a yeast cyclic AMP-dependent protein kinase defect by overexpression of SOK1, a yeast gene exhibiting sequence similarity to a developmentally regulated mouse gene.

机译：通过过表达SOK1来抑制酵母环状AMP依赖性蛋白激酶缺陷，SOK1是与发育受调控的小鼠基因具有序列相似性的酵母基因。

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摘要

Saccharomyces cerevisiae cyclic AMP-dependent protein kinase (A kinase) activity is essential for growth and cell cycle progression. Dependence on A kinase function can be partially relieved by the inactivation of a second kinase encoded by the gene YAK1. We have isolated two new genes, SOK1 and SOK2 (suppressor of kinase), as gene dosage suppressors of the conditional growth defect of several temperature-sensitive A kinase mutants. Overexpression of SOK1, like lesions in YAK1, also restores growth to a strain (tpk1 tpk2 tpk3) lacking all A kinase activity. The SOK1 gene is not essential, but a sok1::HIS3 disruption abrogates suppression of an A kinase defect by yak1. These results suggest that Yak1 and Sok1 define a linear pathway that is partially redundant with that of the A kinase. Activation of Sok1, by SOK1 overexpression or by inactivation of the negative regulator Yak1, renders a cell independent of A kinase function. The implications of such a model are particularly intriguing in light of the nuclear localization pattern of the overexpressed Sok1 protein and the primary sequence homology between SOK1 and a recently described, developmentally regulated mouse gene.
机译：酿酒酵母环状AMP依赖性蛋白激酶（A激酶）活性对于生长和细胞周期进程至关重要。通过使基因YAK1编码的第二种激酶失活，可以部分缓解对A激酶功能的依赖性。我们已经分离出两个新基因，SOK1和SOK2（激酶的抑制剂），作为几种温度敏感A激酶突变体的条件生长缺陷的基因剂量抑制剂。像YAK1中的病变一样，SOK1的过表达也恢复了缺乏所有A激酶活性的菌株（tpk1 tpk2 tpk3）的生长。 SOK1基因不是必需的，但是sok1 :: HIS3破坏可消除yak1对A激酶缺陷的抑制作用。这些结果表明Yak1和Sok1定义了一条线性途径，与A激酶的途径部分重复。通过SOK1过表达或通过负调节子Yak1的失活激活Sok1，使细胞独立于A激酶功能。鉴于过表达的Sok1蛋白的核定位模式以及SOK1与最近描述的，发育受调控的小鼠基因之间的主要序列同源性，这种模型的意义尤其令人着迷。

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