Bender R A, Magasanik B
J Bacteriol. 1977 Oct;132(1):106-12. doi: 10.1128/jb.132.1.106-112.1977.
We isolated an F' episome of Escherichia coli carrying the glnA+ gene from K. aerogenes and an F' episome of E. coli carrying the glnA4 allele from K. aerogenes responsible for the constitutive synthesis of glutamine synthetase. Complementation tests with these episomes showed that the glnA4 mutation (leading to the constitutive synthesis of active glutamine synthetase) was in the gene identified by mutations glnA20, glnA51, and glnA5 as the structural gene for glutamine synthetase. By using these merodiploid strains we were able to show that the glnA51 mutation lead to the synthesis of a glutamine synthetase that lacked enzymatic activity but fully retained its regulatory properties. Finally, we discuss a model that explains the several phenotypes associated with mutations such as glnA4 located within the structural gene for glutamine synthetase leading to constitutive synthesis of active glutamine synthetase.
我们从产气克雷伯菌中分离出携带谷氨酰胺合成酶基因(glnA⁺)的大肠杆菌F'附加体,以及从产气克雷伯菌中分离出携带负责谷氨酰胺合成酶组成型合成的glnA4等位基因的大肠杆菌F'附加体。用这些附加体进行的互补试验表明,glnA4突变(导致活性谷氨酰胺合成酶的组成型合成)位于由glnA20、glnA51和glnA5突变鉴定为谷氨酰胺合成酶结构基因的基因中。通过使用这些部分二倍体菌株,我们能够证明glnA51突变导致合成一种缺乏酶活性但完全保留其调节特性的谷氨酰胺合成酶。最后,我们讨论了一个模型,该模型解释了与位于谷氨酰胺合成酶结构基因内导致活性谷氨酰胺合成酶组成型合成的突变(如glnA4)相关的几种表型。