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Requirement of the Receiver and Phosphotransfer Domains of ArcB for Efficient Dephosphorylation of Phosphorylated ArcA In Vivo

机译:ArcB的受体和磷酸转移域对磷酸化ArcA体内有效脱磷酸作用的要求

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摘要

The Arc two-component system, comprising the ArcB sensor kinase and the ArcA response regulator, modulates the expression of numerous genes in response to the respiratory conditions of growth. Under anoxic growth conditions, ArcB autophosphorylates and transphosphorylates ArcA, which in turn represses or activates its target operons. Under aerobic growth conditions, phosphorylated ArcA (ArcA-P) dephosphorylates and its transcriptional regulation is released. The dephosphorylation of ArcA-P has been shown to occur, at least in vitro, via an ArcAAsp54-P → ArcBHis717-P → ArcBAsp576-P → Pi reverse phosphorelay. In this study, the physiological significance of this pathway was assessed. The results demonstrate that the receiver and phosphotransfer domains of the tripartite sensor kinase ArcB are necessary and sufficient for efficient ArcA-P dephosphorylation in vivo.
机译:包含ArcB传感器激酶和ArcA反应调节剂的Arc两组分系统可响应呼吸的生长条件来调节众多基因的表达。在缺氧的生长条件下,ArcB会自磷酸化和反磷酸化ArcA,从而反过来抑制或激活其靶操纵子。在有氧生长条件下,磷酸化的ArcA(ArcA-P)去磷酸化并释放其转录调控。已显示,至少在体外,ArcA-P的去磷酸化是通过ArcA Asp54 -P→ArcB His717 -P→ArcB Asp576 发生的。 sup> -P→Pi反向磷光。在这项研究中,评估了该途径的生理学意义。结果表明,三方传感器激酶ArcB的受体和磷酸转移域对于体内有效的ArcA-P脱磷酸作用是必要和充分的。

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