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首页> 美国卫生研究院文献>Journal of Bacteriology >Domain Analysis of ArcS the Hybrid Sensor Kinase of the Shewanella oneidensis MR-1 Arc Two-Component System Reveals Functional Differentiation of Its Two Receiver Domains
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Domain Analysis of ArcS the Hybrid Sensor Kinase of the Shewanella oneidensis MR-1 Arc Two-Component System Reveals Functional Differentiation of Its Two Receiver Domains

机译：圆弧菌（Shewanella oneidensis MR-1电弧两组分系统的混合传感器激酶）ArcS的域分析揭示了其两个接收域的功能差异

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摘要

In all species of the genus Shewanella, the redox-sensing Arc two-component system consists of the response regulator ArcA, the sensor kinase ArcS, and the separate phosphotransfer protein HptA. Compared to its counterpart ArcB in Escherichia coli, ArcS has a significantly different domain structure. Resequencing and reannotation revealed that in the N-terminal part, ArcS possesses a periplasmic CaChe-sensing domain bracketed by two transmembrane domains and, moreover, that ArcS has two cytoplasmic PAS-sensing domains and two receiver domains, compared to a single one of each in ArcB. Here, we used a combination of in vitro phosphotransfer studies on purified proteins and phenotypic in vivo mutant analysis to determine the roles of the different domains in ArcS function. The analysis revealed that phosphotransfer occurs from and toward the response regulator ArcA and involves mainly the C-terminal RecII domain. However, RecI also can receive a phosphate from HptA. In addition, the PAS-II domain, located upstream of the histidine kinase domain, is crucial for function. The results support a model in which phosphorylation of RecI stimulates histidine kinase activity of ArcS in order to maintain an appropriate level of phosphorylated ArcA according to environmental conditions. In addition, the study reveals some fundamental mechanistic differences between ArcS/HptA and ArcB with respect to signal perception and phosphotransfer despite functional conservation of the Arc system in Shewanella and E. coli.
机译：在希瓦氏菌属的所有物种中，氧化还原感应弧两组分系统由响应调节剂ArcA，传感器激酶ArcS和单独的磷酸转移蛋白HptA组成。与大肠杆菌中的ArcB相比，ArcS具有明显不同的域结构。重新测序和重新注释表明，在N末端部分，ArcS拥有一个由两个跨膜结构域包围的周质CaChe感应域，此外，与每个单独的一个相比，ArcS具有两个胞质PAS感应域和两个接收器域。在ArcB中。在这里，我们结合了对纯化蛋白的体外磷酸转移研究和表型体内突变体分析，以确定在ArcS功能中不同域的作用。分析表明，磷酸转移是从反应调节剂ArcA发生的，并且主要是向C末端的RecII结构域转移。但是，RecI也可以从HptA接收磷酸盐。另外，位于组氨酸激酶结构域上游的PAS-II结构域对功能至关重要。结果支持了一个模型，其中RecI的磷酸化刺激ArcS的组氨酸激酶活性，以便根据环境条件维持适当水平的磷酸化ArcA。此外，该研究揭示了尽管Shewanella和E.coli中Arc系统功能保守，但ArcS / HptA和ArcB在信号感知和磷转移方面存在一些基本的机械差异。

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