ArticleBMC microbiology2011
Detection and function of an intramolecular disulfide bond in the pH-responsive CadC of Escherichia coli.
Article in BMC microbiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 39 citations in OpenAlex.
- Engineering oncolytic bacteria as precision cancer therapeutics: design principles, therapeutic strategies, and translational perspectives.Protein & cell · 2026Review
- Molecular mechanism of proteolytic cleavage-dependent activation of CadC-mediated response to acid in E. coli.Communications biology · 2024Article
- Co-component signal transduction systems: Fast-evolving virulence regulation cassettes discovered in enteric bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- HAntioxidants (Basel, Switzerland) · 2021Article
- Comparative Review of the Responses ofGenes · 2020Review
- Host stimuli and operator binding sites controlling protein interactions between virulence master regulator ToxR and ToxS in Vibrio cholerae.Molecular microbiology · 2020Article
- A Disulfide Oxidoreductase (CHU_1165) Is Essential for Cellulose Degradation by Affecting Outer Membrane Proteins in Cytophaga hutchinsonii.Applied and environmental microbiology · 2020Article
- The 58th Cysteine of TcpP Is Essential forFrontiers in microbiology · 2020Article
- Sub-lethal Concentrations of Phytochemicals (Carvacrol and Oregano) Select for Reduced Susceptibility Mutants ofPolish journal of microbiology · 2020Article
- Ssy5 is a signaling serine protease that exhibits atypical biogenesis and marked S1 specificity.The Journal of biological chemistry · 2018Article
- Vibrio parahaemolyticus VtrA is a membrane-bound regulator and is activated via oligomerization.PloS one · 2017Article
- Crystal Structure and Conformational Change Mechanism of a Bacterial Nramp-Family Divalent Metal Transporter.Structure (London, England : 1993) · 2016Article
- Thiol-based switch mechanism of virulence regulator AphB modulates oxidative stress response in Vibrio cholerae.Molecular microbiology · 2016Article
- Differential Thiol-Based Switches Jump-Start Vibrio cholerae Pathogenesis.Cell reports · 2016Article
- Vibrio cholerae leuO Transcription Is Positively Regulated by ToxR and Contributes to Bile Resistance.Journal of bacteriology · 2015Article
- AguR, a Transmembrane Transcription Activator of the Putrescine Biosynthesis Operon in Lactococcus lactis, Acts in Response to the Agmatine Concentration.Applied and environmental microbiology · 2015Article
- Topology, dimerization, and stability of the single-span membrane protein CadC.Journal of molecular biology · 2014Article
- The conformational bases for the two functionalities of 2-cysteine peroxiredoxins as peroxidase and chaperone.Journal of experimental botany · 2013Article
- Three-component lysine/ornithine decarboxylation system in Lactobacillus saerimneri 30a.Journal of bacteriology · 2013Article
- Protein disulfide isomerases contribute differentially to the endoplasmic reticulum-associated degradation of apolipoprotein B and other substrates.Molecular biology of the cell · 2012Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundIn an acidic and lysine-rich environment Escherichia coli induces expression of the cadBA operon which encodes CadA, the lysine decarboxylase, and CadB, the lysine/cadaverine antiporter. cadBA expression is dependent on CadC, a membrane-integrated transcriptional activator which belongs to the ToxR-like protein family. Activation of CadC requires two stimuli, lysine and low pH. Whereas lysine is detected by an interplay between CadC and the lysine-specific transporter LysP, pH alterations are sensed by CadC directly. Crystal structural analyses revealed a close proximity between two periplasmic cysteines, Cys208 and Cys272.
resultsSubstitution of Cys208 and/or Cys272 by alanine resulted in CadC derivatives that were active in response to only one stimulus, either lysine or pH 5.8. Differential in vivo thiol trapping revealed a disulfide bond between these two residues at pH 7.6, but not at pH 5.8. When Cys208 and Cys272 were replaced by aspartate and lysine, respectively, virtually wild-type behavior was restored indicating that the disulfide bond could be mimicked by a salt bridge.
conclusionA disulfide bond was found in the periplasmic domain of CadC that supports an inactive state of CadC at pH 7.6. At pH 5.8 disulfide bond formation is prevented which transforms CadC into a semi-active state. These results provide new insights into the function of a pH sensor.
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