THE CARBOXY-TERMINAL 30 AMINO-ACIDS OF GAL4 ARE RECOGNIZED BY GAL80
THE CARBOXY-TERMINAL 30 AMINO-ACIDS OF GAL4 ARE RECOGNIZED BY GAL80
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DOI：
10.1016/0092-8674(87)90670-2
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发表时间：
1987-07-03
期刊：
影响因子：
64.5
通讯作者：
PTASHNE, M
中科院分区：
文献类型：
--
作者：
MA, J;PTASHNE, M
在野生型酵母中，转录激活剂 GAL4 的作用被 GAL80 抑制，而半乳糖可以缓解这种抑制。我们发现，缺乏羧基末端 30 个氨基酸的 GAL4 缺失突变体会组成型激活转录，而其他带有羧基末端 30 个氨基酸的缺失突变体则被 GAL80 抑制。此外，当从多拷贝质粒上的强启动子表达时，带有这30个氨基酸的GAl4片段使内源GAL4免受GAL80的抑制。这些和其他结果表明，GAL80 识别 GAL4 的羧基端 30 个氨基酸，形成复合物，虽然与 DNA 结合，但不会激活转录。
In wild-type yeast the action of the transcriptional activator GAL4 is inhibited by GAL80, and galactose relieves this inhibition. We show that deletion mutants of GAL4 lacking 30 amino acids of the carboxyl terminus activate transcription constitutively, whereas other deletion mutants bearing the carboxy-terminal 30 amino acids are inhibited by GAL80. Moreover, GAl4 fragments bearing these 30 amino acids, when expressed from a strong promoter on multicopy plasmide, free the endogenous GAL4 from inhibition by GAL80. These and other results suggest that GAL80 recognizes the carboxy-terminal 30 amino acids of GAL4, forming a complex that, though bound to DNA, does not activate transcription.