ACTIVATION OF BACTERIAL PORIN GENE-EXPRESSION BY A CHIMERIC SIGNAL TRANSDUCER IN RESPONSE TO ASPARTATE
ACTIVATION OF BACTERIAL PORIN GENE-EXPRESSION BY A CHIMERIC SIGNAL TRANSDUCER IN RESPONSE TO ASPARTATE
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DOI：
10.1126/science.2476847
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发表时间：
1989-09-15
期刊：
影响因子：
56.9
通讯作者：
INOUYE, M
中科院分区：
文献类型：
--
作者：
UTSUMI, R;BRISSETTE, RE;INOUYE, M
大肠杆菌的焦油趋化受体是一种膜结合的感觉蛋白，促进细菌对天冬氨酸的趋化反应。EnvZ分子具有与Tar相似的膜拓扑结构，被认为是一种渗透传感器，是主要外膜孔蛋白OmpF和OmpC基因渗透调节所必需的。Tar的胞质信号域被EnvZ的羧基部分取代，由此产生的嵌合受体激活了ompC基因的转录，以响应天冬氨酸。嵌合受体对ompC的激活完全依赖于OmpR，它是ompF和ompC的转录激活因子。
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.