Leuther K K, Salmeron J M, Johnston S A
Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas 75235-8573.
Cell. 1993 Feb 26;72(4):575-85. doi: 10.1016/0092-8674(93)90076-3.
Regulation of gene expression in eukaryotes relies on intricate protein-protein interactions. Transcription of the galactose genes in yeast has been a productive model for this type of interaction. The positive activator in this system, GAL4, has a bifunctional C-terminus. It contains both a prototypic acidic activation domain and a region that binds the negative regulator, GAL80. We have taken advantage of this colocalization of functions to subject the region to a constrained mutagenesis analysis: one function was maintained, while the other one was altered. This analysis and the experiments it suggested have led us to two conclusions: first, the acidic amino acids are not, as commonly thought, required for activation; second, this region is not unstructured or alpha helical, but its function may require a beta sheet.
真核生物中基因表达的调控依赖于复杂的蛋白质-蛋白质相互作用。酵母中半乳糖基因的转录一直是这类相互作用的一个有效模型。该系统中的正激活因子GAL4具有双功能的C末端。它既包含一个典型的酸性激活结构域,又包含一个与负调控因子GAL80结合的区域。我们利用这种功能的共定位对该区域进行了受限诱变分析:保持一种功能,同时改变另一种功能。这一分析及其所建议的实验使我们得出两个结论:第一,激活作用并不像通常认为的那样需要酸性氨基酸;第二,该区域并非无结构或呈α螺旋状,但其功能可能需要β折叠。