The Aer protein and the serine chemoreceptor Tsr independently sense intracellular energy levels and transduce oxygen, redox, and energy signals for Escherichia coli behavior
The Aer protein and the serine chemoreceptor Tsr independently sense intracellular energy levels and transduce oxygen, redox, and energy signals for Escherichia coli behavior
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DOI：
10.1073/pnas.94.20.10541
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发表时间：
1997-09-30
影响因子：
11.1
通讯作者：
Taylor, BL
中科院分区：
文献类型：
--
作者：
Rebbapragada, A;Johnson, MS;Taylor, BL
我们发现了一种蛋白质Aer，它是一种信号转导器，可以感知细胞内的能量水平，而不是外部环境，并为趋氧性转导信号Aer的结构域与趋化性受体的信号结构域和某些转录激活因子的氧敏感结构域相似，Aer的N-末端结构域中推定的FAD结合位点与NifL、Bat和Wc-1信号转导蛋白共享共有序列，所述NifL、Bat和Wc-1信号转导蛋白分别响应于氧化还原变化、氧和蓝光调节基因表达。对嗜氧性、氧化还原性和甘油的趋化性均呈阴性，每一种趋化性都需要质子动力和/或电子传递系统来传递信号。我们认为，Aer和Tsr感知质子动力或细胞氧化还原状态，从而整合了引导E.大肠杆菌的环境中，最大的能量是可用于生长。
We identified a protein, Aer, as a signal transducer that senses intracellular energy levels rather than the external environment and that transduces signals for aerotaxis (taxis to oxygen) and other energy-dependent behavioral responses in Escherichia coli, Domains in Aer are similar to the signaling domain in chemotaxis receptors and the putative oxygen-sensing domain of some transcriptional activators, A putative FAD-binding site in the N-terminal domain of Aer shares a consensus sequence with the NifL, Bat, and Wc-1 signal-transducing proteins that regulate gene expression in response to redox changes, oxygen, and blue light, respectively, A double mutant deficient in aer and tsr, which codes for the serine chemoreceptor, was negative for aerotaxis, redox taxis, and glycerol taxis, each of which requires the proton motive force and/or electron transport system for signaling, We propose that Aer and Tsr sense the proton motive force or cellular redox state and thereby integrate diverse signals that guide E. coli to environments where maximal energy is available for growth.