邻氨基苯甲酸合酶亚基的属间互补作用
Intergeneric complementation of anthranilate synthase subunits.
作者信息
Patel N, Holmes W M, Kane J F
出版信息
J Bacteriol. 1973 May;114(2):600-2. doi: 10.1128/jb.114.2.600-602.1973.
Partially purified subunits of anthranilate synthase were prepared from Bacillus subtilis and Pseudomonas aeruginosa. The large component from B. subtilis (I(B)) complements well with the small component from P. aeruginosa (II(P)) to reconstitute a glutamine-reactive anthranilate synthase. This interaction can be demonstrated with crude extracts from a B. subtilis trpX mutant and a P. aeruginosa trpA mutant. Complementation was also observed with the large component from P. aeruginosa (I(P)) and the small subunit from B. subtilis (II(B)). At saturation the heterologous complex I(B)II(P) has 93% of the activity of the homologous complex I(B)II(B), whereas the hybrid I(P)II(B) is only 22% as active as the homologous complex I(P)II(P).
从枯草芽孢杆菌和铜绿假单胞菌中制备了部分纯化的邻氨基苯甲酸合酶亚基。枯草芽孢杆菌的大亚基（I(B)）与铜绿假单胞菌的小亚基（II(P)）能很好地互补，以重构一种对谷氨酰胺有反应的邻氨基苯甲酸合酶。这种相互作用可用枯草芽孢杆菌trpX突变体和铜绿假单胞菌trpA突变体的粗提取物来证明。用铜绿假单胞菌的大亚基（I(P)）和枯草芽孢杆菌的小亚基（II(B)）也观察到了互补作用。在饱和状态下，异源复合物I(B)II(P)具有同源复合物I(B)II(B)活性的93%，而杂合复合物I(P)II(B)的活性仅为同源复合物I(P)II(P)的22%。
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