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
R Malpica; B Franco; C Rodriguez; Oh Suk Kwon; D Georgellis
Bibliographic Citation
Proceedings of National Academy of Sciences of United States of America, vol. 101, no. 36, pp. 13318-13323
Publication Year
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.
Natl Acad Sciences
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Division of Bio Technology Innovation > SME Support Center > 1. Journal Articles
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