ArticleThe Journal of biological chemistry2011
New insights into the signaling mechanism of the pH-responsive, membrane-integrated transcriptional activator CadC of Escherichia coli.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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37 citing papers in PubMed, 63 citations in OpenAlex.
- AdiY acts as a cytoplasmic pH sensor via histidine protonation to regulate acid stress adaptation inJournal of bacteriology · 2026Article
- Development of a lysine biosensor for the dynamic regulation of cadaverine biosynthesis in E. coli.Microbial cell factories · 2025Article
- Evolution of pH-sensitive transcription termination inProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Review
- A critical role for iron and zinc homeostatic systems in the evolutionary adaptation ofMicrobial genomics · 2023Article
- The Interplay of AphB and CadC to Activate Acid Resistance ofJournal of bacteriology · 2023Article
- Chitinase A, a tightly regulated virulence factor of Salmonella enterica serovar Typhimurium, is actively secreted by a Type 10 Secretion System.PLoS pathogens · 2023Article
- Characterization of Eight Bacterial Biosensors for Microbial Diagnostic and Therapeutic Applications.ACS synthetic biology · 2022Article
- Sequestration of a dual function DNA-binding protein byProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Division of labor and collective functionality in Escherichia coli under acid stress.Communications biology · 2022Article
- Cytotoxic Minor Piericidin Derivatives from the Actinomycete StrainMarine drugs · 2021Article
- Dynamic relocalization of cytosolic type III secretion system components prevents premature protein secretion at low external pH.Nature communications · 2021Article
- The enigma of environmental pH sensing in plants.Nature plants · 2021Review
- Dynamics of chromosomal target search by a membrane-integrated one-component receptor.PLoS computational biology · 2021Article
- Comparative Review of the Responses ofGenes · 2020Review
- Molecular design of a signaling system influences noise in protein abundance under acid stress in different γ-Proteobacteria.Journal of bacteriology · 2020Article
- Dropping Out and Other Fates of Transmembrane Segments Inserted by the SecA ATPase.Journal of molecular biology · 2019Article
- DNA-binding directs the localization of a membrane-integrated receptor of the ToxR family.Communications biology · 2019Article
- Protein Activity Sensing in Bacteria in Regulating Metabolism and Motility.Frontiers in microbiology · 2019Review
- Review
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The membrane-integrated transcriptional regulator CadC of Escherichia coli activates expression of the cadBA operon at low external pH with concomitantly available lysine, providing adaptation to mild acidic stress. CadC is a representative of the ToxR-like proteins that combine sensory, signal transduction, and DNA-binding activities within a single polypeptide. Although several ToxR-like regulators such as CadC, as well as the main regulator of Vibrio cholerae virulence, ToxR itself, which activate gene expression at acidic pH, have been intensively investigated, their molecular activation mechanism is still unclear. In this study, a structure-guided mutational analysis was performed to elucidate the mechanism by which CadC detects acidification of the external milieu. Thus, a cluster of negatively charged amino acids (Asp-198, Asp-200, Glu-461, Glu-468, and Asp-471) was found to be crucial for pH detection. These amino acids form a negatively charged patch on the surface of the periplasmic domain of CadC that stretches across its two subdomains. The results of different combinations of amino acid replacements within this patch indicated that the N-terminal subdomain integrates and transduces the signals coming from both subdomains to the transmembrane domain. Alterations in the phospholipid composition did not influence pH-dependent cadBA expression, and therefore, interplay of the acidic surface patch with the negatively charged headgroups is unlikely. Models are discussed according to which protonation of these acidic amino acid side chains reduces repulsive forces between the two subdomains and/or between two monomers within a CadC dimer and thereby enables receptor activation upon lowering of the environmental pH.
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