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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Identification of a quinone-sensitive redox switch in the ArcB sensor kinase.
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Identification of a quinone-sensitive redox switch in the ArcB sensor kinase.

机译：识别ArcB传感器激酶中醌敏感的氧化还原开关。

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摘要

Escherichia coli senses and signals anoxic or low redox conditions in its growth environment by the Arc two-component system. Under anaerobic conditions, the ArcB sensor kinase autophosphorylates and transphosphorylates ArcA, a global transcriptional regulator that controls the expression of numerous operons involved in respiratory or fermentative metabolism. Under aerobic conditions, the kinase activity of ArcB is inhibited by the quinone electron carriers that act as direct negative signals. Here, we show that the molecular mechanism of kinase silencing involves the oxidation of two cytosol-located redox-active cysteine residues that participate in intermolecular disulfide bond formation, a reaction in which the quinones provide the source of oxidative power. Thus, a pivotal link in the Arc signal transduction pathway connecting the redox state of the quinone pool to the transcriptional apparatus is elucidated.
机译：大肠杆菌通过Arc两组分系统在其生长环境中感知并发出缺氧或低氧化还原条件并发出信号。在厌氧条件下，ArcB传感器激酶可自磷酸化和反磷酸化ArcA，ArcA是一种全局转录调节因子，可控制参与呼吸或发酵代谢的许多操纵子的表达。在有氧条件下，充当直接负信号的醌电子载体抑制了ArcB的激酶活性。在这里，我们表明激酶沉默的分子机制涉及参与分子间二硫键形成的两个位于胞浆中的氧化还原活性半胱氨酸残基的氧化，其中醌提供了氧化能力的来源。因此，阐明了在电弧信号传导途径中将醌池的氧化还原状态连接到转录装置的关键连接。

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