FUNCTIONAL DISSECTION OF A EUKARYOTIC TRANSCRIPTIONAL ACTIVATOR PROTEIN, GCN4 OF YEAST
FUNCTIONAL DISSECTION OF A EUKARYOTIC TRANSCRIPTIONAL ACTIVATOR PROTEIN, GCN4 OF YEAST
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DOI：
10.1016/0092-8674(86)90070-x
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发表时间：
1986-09-12
期刊：
影响因子：
64.5
通讯作者：
STRUHL, K
中科院分区：
文献类型：
--
作者：
HOPE, IA;STRUHL, K
酵母GCN 4蛋白特异性结合氨基酸生物合成基因的启动子并协同诱导其转录。连续缺失的GCN 4和杂合LexA-GCN 4蛋白在体外测定特异性DNA结合活性，并在体内刺激转录。特异性DNA结合活性存在于GCN 4的60个C-末端氨基酸，即碱性区域。然而，含有整个DNA结合区的某些缺失不能激活转录，而是在体内充当阻遏物。活化功能似乎关键地涉及仅19个氨基酸，这些氨基酸集中位于GCN 4的酸性区域中。除了它们的功能分离之外，蛋白质的DNA结合区和转录激活区可以通过弹性蛋白酶切割物理分离。这些结果的DNA序列识别和转录激活的机制的影响进行了讨论。
Yeast GCN4 protein binds specifically to the promoters of amino acid biosynthetic genes and coordinately induces their transcription. Serially deleted GCN4 and hybrid LexA-GCN4 proteins were assayed for specific DNA binding activity in vitro, and for stimulation of transcription in vivo. The specific DNA binding activity resides in the 60 C-terminal amino acids, a basic region of GCN4. However, certain deletions containing the entire DNA binding region are unable to activate transcription and instead act as repressors in vivo. The activation function appears to critically involve just 19 amino acids that are centrally located in an acidic region of GCN4. In addition to their functional separation, the DNA binding and transcriptional activation regions of the protein can be separated physically by elastase cleavage. The implications of these results for the mechanisms of DNA sequence recognition and transcription activation are discussed.