Dorrington R A, Cooper T G
Department of Microbiology and Immunology, University of Tennessee, Memphis 38163.
Nucleic Acids Res. 1993 Aug 11;21(16):3777-84. doi: 10.1093/nar/21.16.3777.
Expression of the DAL2, DAL4, DAL7, DUR1,2, and DUR3 genes in S. cerevisiae is induced by allophanate, the last intermediate in the allantoin catabolic pathway. Analysis of the DAL7 promoter identified a dodecanucleotide, the DAL7 UIS, which was required for inducer-responsiveness. Operation of the DAL7 UIS required functional DAL81 and DAL82 gene products. Since the DAL81 product was not an allantoin pathway-specific regulatory factor, the DAL82 product was considered as the more likely candidate to be the DAL UIS binding protein. Using an E. coli expression system, we showed that DAL82 protein specifically bound to wild type but not mutant DAL UIS sequences. DNA fragments containing DAL UIS elements derived from various DAL gene promoters bound DAL82 protein with different affinities which correlate with the degree of inducer-responsiveness the genes displayed.
在酿酒酵母中，尿囊素分解代谢途径的最后中间体脲基甲酸可诱导DAL2、DAL4、DAL7、DUR1,2和DUR3基因的表达。对DAL7启动子的分析鉴定出一个十二核苷酸，即DAL7上游诱导序列（DAL7 UIS），它是诱导物应答所必需的。DAL7 UIS的运作需要功能性的DAL81和DAL82基因产物。由于DAL81产物不是尿囊素途径特异性调节因子，因此DAL82产物被认为更有可能是DAL UIS结合蛋白。使用大肠杆菌表达系统，我们发现DAL82蛋白特异性结合野生型而非突变型DAL UIS序列。含有源自各种DAL基因启动子的DAL UIS元件的DNA片段以不同亲和力结合DAL82蛋白，这与这些基因所表现出的诱导物应答程度相关。
