Davidson J P, Wilson D J
Tuskeegee University, Department of Biology, Alabama 36088.
Biochem Biophys Res Commun. 1991 Aug 15;178(3):934-9. doi: 10.1016/0006-291x(91)90981-c.
Concerted efforts were directed towards understanding the control of acetohydroxy acid synthase (AHAS) in the gyrB mutant hisU1820 of Salmonella typhimurium. A media shift from valine to valine plus isoleucine causes a dramatic 4 to 5 fold burst of AHAS valine sensitive activity which appears to be dependent on translation. DJ19, an isolated valine sensitive derivative of the gyrB mutant, maintains a dramatic increase in AHAS valine sensitive activity upon the addition of isoleucine to valine supplemented cultures, suggesting that the isoleucine effect is specific for valine sensitive AHAS. Evidence supports isoleucine as a positive effector on valine sensitive AHAS expression and that the gyrB mutation accentuates the isoleucine effect.
研究人员齐心协力,致力于了解鼠伤寒沙门氏菌gyrB突变体hisU1820中乙酰羟酸合酶(AHAS)的调控机制。培养基从含有缬氨酸转变为含有缬氨酸加异亮氨酸时,AHAS缬氨酸敏感活性会出现4到5倍的急剧爆发,这种爆发似乎依赖于翻译过程。DJ19是从gyrB突变体中分离出的缬氨酸敏感衍生物,在缬氨酸补充培养基中添加异亮氨酸后,其AHAS缬氨酸敏感活性会显著增加,这表明异亮氨酸对缬氨酸敏感的AHAS具有特异性作用。有证据支持异亮氨酸作为缬氨酸敏感AHAS表达的正效应物,且gyrB突变会增强异亮氨酸的作用效果。