Ito Tatsuo, Tani Shuji, Itoh Tomoyuki, Tsukagoshi Norihiro, Kato Masashi, Kobayashi Tetsuo
Department of Biological Mechanisms and Functions, Graduate School of Bioagricultural Sciences, Nagoya University, Chikusa-ku, Japan.
Biosci Biotechnol Biochem. 2004 Sep;68(9):1906-11. doi: 10.1271/bbb.68.1906.
AmyR is a transcriptional activator in Aspergillus spp. necessary for induction of the amylolytic enzyme genes. It recognizes 5'-CGGN8CGG-3' conserved in a number of the amylolytic gene promoters, and in addition 5'-CGGAAATTTAA-3' in the A. oryzae alpha-amylase promoter. In this report, interaction of AmyR with the 5'-CGGAAATTTAA-3' type binding site in the Taka-amylase gene (taaG2) promoter was precisely characterized by DNase I footprinting analysis and electrophoretic mobility shift assay in vitro, and also by examination of the in vivo activity of the mutated promoters. The in vitro and in vivo analyses indicated that two AmyR molecules bind cooperatively to the 5'-CGGAAATTTAA-3' sequence by recognizing the CGG triplet at the 5'-end and the AGG triplet just downstream of the sequence.
AmyR是曲霉属中的一种转录激活因子，对于诱导淀粉酶基因是必需的。它识别许多淀粉酶基因启动子中保守的5'-CGGN8CGG-3'，此外还识别米曲霉α-淀粉酶启动子中的5'-CGGAAATTTAA-3'。在本报告中，通过体外DNase I足迹分析和电泳迁移率变动分析，以及对突变启动子的体内活性检测，精确表征了AmyR与Taka淀粉酶基因（taaG2）启动子中5'-CGGAAATTTAA-3'型结合位点的相互作用。体外和体内分析表明，两个AmyR分子通过识别序列5'-端的CGG三联体和该序列下游紧邻的AGG三联体，协同结合到5'-CGGAAATTTAA-3'序列上。
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