Stanway C, Mellor J, Ogden J E, Kingsman A J, Kingsman S M
Department of Biochemistry, University of Oxford, UK.
Nucleic Acids Res. 1987 Sep 11;15(17):6855-73. doi: 10.1093/nar/15.17.6855.
The upstream activation site (UAS) of the yeast phosphoglycerate kinase gene (PGK) has been localised by deletion analysis (1). Here we show that the UASPGK contains two functionally distinct domains. These two domains, designated activator (A) and modulator (M), appear to be located within bases -460 to -402 and -531 to -461, respectively, relative to the initiating ATG; although it is possible that part of the M domain resides within the A domain. They have been shown, using a heterologous assay promoter, to have distinct transcriptional functions. Domain A is responsible for activation of transcription whilst domain M is required for carbon source dependent regulation of transcription. Protein-DNA binding studies have demonstrated that the DNA fragment containing domain M has high affinity for at least one specific DNA-binding protein, whilst domain A does not appear to interact strongly in protein-binding assays under the same conditions. The domain M binding activity is dependent on the carbon source in the growth medium and may be functional in the carbon source control of PGK expression.
酵母磷酸甘油酸激酶基因（PGK）的上游激活位点（UAS）已通过缺失分析进行了定位（1）。在此我们表明，UASPGK包含两个功能不同的结构域。这两个结构域，分别命名为激活子（A）和调节子（M），相对于起始ATG，似乎分别位于碱基-460至-402和-531至-461之间；尽管M结构域的一部分可能位于A结构域内。使用异源分析启动子已表明它们具有不同的转录功能。结构域A负责转录激活，而结构域M是碳源依赖性转录调控所必需的。蛋白质-DNA结合研究表明，包含结构域M的DNA片段对至少一种特定的DNA结合蛋白具有高亲和力，而在相同条件下，结构域A在蛋白质结合分析中似乎没有强烈的相互作用。结构域M的结合活性取决于生长培养基中的碳源，并且可能在PGK表达的碳源控制中起作用。
