Bolotin A, Khazak V, Stoynova N, Ratmanova K, Yomantas Y, Kozlov Y
Department of Biotechnology, Research Institute of Genetics and Selection of Industrial Micro-organisms (GNIIgenetika), Moscow, Russia.
Microbiology (Reading). 1995 Sep;141 ( Pt 9):2219-22. doi: 10.1099/13500872-141-9-2219.
A DNA fragment containing the aroA(G) gene of Bacillus subtilis 168, encoding 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) synthase-chorismate mutase, was cloned and sequenced. The N-terminus of the protein encoded by aroA(G) showed homology with chorismate mutase encoded by aroH of B. subtilis and with the chorismate mutase parts of proteins encoded by the pheA and tyrA genes of Escherichia coli. The C-terminus of the aroA(G) product has sequence similarity with 3-deoxy-D-manno-octulosonate 8-phosphate synthase of E. coli. It was shown that the proteins encoded by the aroA(G) gene of B. subtilis 168 and the aroA gene of B. subtilis ATCC 6051 Marburg strain are identical, so the observed differences in DAHP synthase activity from these two strains must result from other changes.
克隆并测序了一段包含枯草芽孢杆菌168的aroA(G)基因的DNA片段,该基因编码3-脱氧-D-阿拉伯庚酮糖酸-7-磷酸(DAHP)合酶-分支酸变位酶。aroA(G)编码的蛋白质的N端与枯草芽孢杆菌aroH编码的分支酸变位酶以及大肠杆菌pheA和tyrA基因编码的蛋白质的分支酸变位酶部分具有同源性。aroA(G)产物的C端与大肠杆菌的3-脱氧-D-甘露辛酮糖酸-8-磷酸合酶具有序列相似性。结果表明,枯草芽孢杆菌168的aroA(G)基因和枯草芽孢杆菌ATCC 6051马尔堡菌株的aroA基因编码的蛋白质是相同的,因此观察到的这两种菌株在DAHP合酶活性上的差异必定是由其他变化导致的。