Detection and function of an intramolecular disulfide bond in the pH-responsive CadC of Escherichia coli
2011
How CadC in E. coli Senses pH and Lysine
publication
Evidence: moderate
Author Information
Author(s): Tetsch Larissa, Koller Christiane, Dönhöfer Alexandra, Jung Kirsten
Primary Institution: Ludwig-Maximilians-Universität München
Hypothesis
The study investigates the role of cysteine residues in the pH-responsive CadC protein of Escherichia coli.
Conclusion
A disulfide bond in CadC is crucial for its function as a pH sensor, affecting its activity based on environmental pH levels.
Supporting Evidence
- CadC contains three cysteine residues, two of which are crucial for its activity.
- A disulfide bond forms at pH 7.6 but is not present at pH 5.8.
- Replacing cysteines with other amino acids can mimic the function of the disulfide bond.
Takeaway
CadC is a protein in E. coli that helps the bacteria respond to changes in pH and lysine levels, and it does this by forming a special bond that changes when the pH changes.
Methodology
The study used site-directed mutagenesis to create CadC derivatives and performed β-galactosidase assays to measure cadBA expression.
Digital Object Identifier (DOI)
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