Utsumi R, Brissette R E, Rampersaud A, Forst S A, Oosawa K, Inouye M
Department of Biochemistry, University of Medicine and Dentistry of New Jersey, Robert Wood Johnson Medical School, Piscataway 08854.
Science. 1989 Sep 15;245(4923):1246-9. doi: 10.1126/science.2476847.
The Tar chemoreceptor of Escherichia coli is a membrane-bound sensory protein that facilitates bacterial chemotaxis in response to aspartate. The EnvZ molecule has a membrane topology similar to Tar and is a putative osmosensor that is required for osmoregulation of the genes for the major outer membrane porin proteins, OmpF and OmpC. The cytoplasmic signaling domain of Tar was replaced with the carboxyl portion of EnvZ, and the resulting chimeric receptor activated transcription of the ompC gene in response to aspartate. The activation of ompC by the chimeric receptor was absolutely dependent on OmpR, a transcriptional activator for ompF and ompC.
大肠杆菌的Tar化学感受器是一种膜结合传感蛋白，可促进细菌对天冬氨酸作出反应的趋化作用。EnvZ分子具有与Tar相似的膜拓扑结构，是一种假定的渗透压感受器，主要外膜孔蛋白OmpF和OmpC的基因渗透调节需要该感受器。Tar的细胞质信号结构域被EnvZ的羧基部分取代，产生的嵌合受体在天冬氨酸的作用下激活了ompC基因的转录。嵌合受体对ompC的激活绝对依赖于OmpR，OmpR是ompF和ompC的转录激活因子。
