Weglenski P, Ninfa A J, Ueno-Nishio S, Magasanik B
Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.
J Bacteriol. 1989 Aug;171(8):4479-85. doi: 10.1128/jb.171.8.4479-4485.1989.
Mutations in the glnG gene of Escherichia coli that result in increased activity of nitrogen regulator I (NRI), the product of glnG, were obtained by two different selection procedures. The mutant proteins were purified and characterized. The concentrations of mutant proteins needed to activate transcription at the glnAp2 promoter were three to four times lower than that of the wild-type NRI. The rate of phosphorylation of these proteins and the stability of mutant NRI phosphate were found to be similar to those of the wild-type NRI. In one of the mutants, the site of the mutation was localized in the DNA region specifying the central domain of NRI.
通过两种不同的筛选程序获得了大肠杆菌谷氨酰胺合成酶基因(glnG)中的突变,这些突变导致谷氨酰胺合成酶基因产物氮调节蛋白I(NRI)的活性增加。对突变蛋白进行了纯化和特性分析。激活glnAp2启动子转录所需的突变蛋白浓度比野生型NRI低三到四倍。发现这些蛋白的磷酸化速率和突变型NRI磷酸盐的稳定性与野生型NRI相似。在其中一个突变体中,突变位点位于指定NRI中央结构域的DNA区域。