Glc8 is a glucose-repressible activator of Glc7 protein phosphatase-1
Glc8 is a glucose-repressible activator of Glc7 protein phosphatase-1
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DOI：
10.1016/s0003-9861(02)00231-x
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发表时间：
2002-08-01
影响因子：
3.9
通讯作者：
Cannon, JF
中科院分区：
文献类型：
--
作者：
Nigavekar, SS;Tan, YSH;Cannon, JF
在芽殖酵母中研究了 Glc7 1 型蛋白磷酸酶稳定性和活性的调节。我们发现Glc7蛋白的半衰期超过180分钟，足够几代人使用。 Glc7 蛋白稳定性在细胞周期和分批培养物生长过程中保持恒定。此外，删除调节亚基 Gac1、Reg1、Reg2、Sds22 或 Glc8 对 Glc7 蛋白半衰期没有影响。作为冈田酸抗性磷酸化酶磷酸酶活性测定的Glc7活性在细胞周期期间是恒定的。删除上述调节亚基表明，只有 Glc8 删除对降低 Glc7 活性有显着影响。 Glc7 活性在稳定期以 Glc8 依赖性方式被诱导。此外，细胞外葡萄糖抑制Glc7活性的诱导。这些结果与葡萄糖对 Glc8 表达的抑制一致，并支持 Glc8 作为主要 Glc7 激活剂的作用。 (C) 2002 年爱思唯尔科学（美国）。版权所有。
Regulation of Glc7 type 1 protein phosphatase stability and activity was studied in budding yeast. We found that the Glc7 protein has a half-life of over 180min, which is sufficient for several generations. Glc7 protein stability was constant during the cell cycle and in batch culture growth. Furthermore, deletion of regulatory subunit Gac1, Reg1, Reg2, Sds22, or Glc8 had no influence on Glc7 protein half-life. The activity of Glc7 assayed as okadaic acid-resistant phosphorylase phosphatase activity was constant during the cell cycle. Deletion of the aforementioned regulatory subunits revealed that only Glc8 deletion had a significant effect in reducing Glc7 activity. Glc7 activity was induced during stationary phase in a Glc8-dependent manner. In addition, extracellular glucose repressed the induction of Glc7 activity. These results are consistent with glucose repression of Glc8 expression and favor the role of Glc8 as a major Glc7 activator. (C) 2002 Elsevier Science (USA). All rights reserved.