Masters P S, Hong J S
J Bacteriol. 1981 Sep;147(3):805-19. doi: 10.1128/jb.147.3.805-819.1981.
The active transport of glutamine by Escherichia coli occurs via a single osmotic shock-sensitive transport system which is known to be dependent upon a periplasmic binding protein specific for glutamine. We obtained a mutant that had elevated levels of glutamine transport and overproduced the glutamine binding protein. From this strain many point mutants and deletion-carrying strains defective in glutamine transport were isolated by a variety of techniques. The genetic locus coding for the glutamine transport system, glnP, and the regulatory mutation which causes overproduction of the transport system were both shown to map at 17.7 min on the E. coli chromosome, and it was demonstrated that the glnP locus contains the structural gene for the glutamine binding protein. Evidence was also obtained that the glutamine transport system, by an unknown mechanism, plays a direct role in the catabolism of glutamate and, hence, of glutamine and proline as well.
大肠杆菌对谷氨酰胺的主动转运是通过单一的对渗透压休克敏感的转运系统进行的,已知该系统依赖于一种对谷氨酰胺具有特异性的周质结合蛋白。我们获得了一个谷氨酰胺转运水平升高且谷氨酰胺结合蛋白过量产生的突变体。通过多种技术从该菌株中分离出了许多谷氨酰胺转运缺陷的点突变体和携带缺失的菌株。编码谷氨酰胺转运系统的基因位点glnP以及导致转运系统过量产生的调控突变均被证明位于大肠杆菌染色体上17.7分钟处,并且证明glnP位点包含谷氨酰胺结合蛋白的结构基因。还获得了证据表明,谷氨酰胺转运系统通过未知机制在谷氨酸的分解代谢中起直接作用,因此在谷氨酰胺和脯氨酸的分解代谢中也起直接作用。