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Updated: Nov 3, 2025

Quantification of Bacterial Histidine Kinase Autophosphorylation Using a Nitrocellulose Binding Assay
Published on: January 11, 2017
Acid-Sensing Histidine Kinase With a Redox Switch.
Shinya Inada1, Toshihide Okajima2, Ryutaro Utsumi2
1Graduate School of Biology-Oriented Science and Technology, Kindai University, Kinokawa, Japan.
The EvgS/EvgA system in Escherichia coli senses acidity. Its activation requires aerobic conditions and ubiquinone, with the PAS domain acting as a redox switch.
Area of Science:
- Microbiology
- Bacterial Physiology
- Signal Transduction
Background:
- The EvgS/EvgA system in Escherichia coli regulates acid resistance genes.
- EvgS, a histidine kinase, has a periplasmic domain for pH sensing and a cytoplasmic PAS domain.
- Previous work suggested the PAS domain's involvement in EvgS activation.
Purpose of the Study:
- To investigate the role of oxygen and ubiquinone in EvgS activation.
- To elucidate the function of the EvgS cytoplasmic PAS domain in signal transduction.
Main Methods:
- EvgS/EvgA reporter assays under varying oxygen conditions.
- Analysis of EvgS mutants (C671A, C683A) in the PAS domain.
- Investigating the requirement of ubiquinone for EvgS activation.
Main Results:
- EvgS activation by mild acidity requires aerobic conditions.
- Mutations in the PAS domain (C671A, C683A) lead to anaerobic EvgS activation.
- Ubiquinone, an electron carrier, is essential for EvgS activation.
Conclusions:
- A model for EvgS activation involving oxidation is proposed.
- The cytoplasmic PAS domain functions as an intermediate redox switch for EvgS activation.
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