Structural and Functional Analysis of the Signal-Transducing Linker in the pH-Responsive One-Component System CadC of Escherichia coli
Abstract
The pH-responsive one-component signaling system CadC in Escherichia coli belongs to the family of ToxR-like proteins, whose members share a conserved modular structure, with an N-terminal cytoplasmic winged helix-turn-helix DNA-binding domain being followed by a single transmembrane helix and a C-terminal periplasmic pH-sensing domain. In E. coli CadC, a cytoplasmic linker comprising approximately 50 amino acids is essential for transmission of the signal from the sensor to the DNA-binding domain. However, the mechanism of transduction is poorly understood. Using NMR spectroscopy, we demonstrate here that the linker region is intrinsically disordered in solution. Furthermore, mutational analyses showed that it tolerates a range of amino acid substitutions (altering polarity, rigidity and α-helix-forming propensity), is robust to extension but is sensitive to truncation. Indeed, truncations either reversed the expression profile of the target operon cadBA or decoupled expression from external pH altogether. CadC dimerizes via its periplasmic domain, but light-scattering analysis provided no evidence for dimerization of the isolated DNA-binding domain, with or without the linker region. However, bacterial two-hybrid analysis revealed that CadC forms stable dimers in a stimulus- and linker-dependent manner, interacting only at pH<6.8. Strikingly, a variant with inversed cadBA expression profile, which lacks most of the linker, dimerizes preferentially at higher pH. Thus, we propose that the disordered CadC linker is required for transducing the pH-dependent response of the periplasmic sensor into a structural rearrangement that facilitates dimerization of the cytoplasmic CadC DNA-binding domain.
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The disordered linker of CadC is required to transduce the pH-dependent status of the periplasmic sensing domain to the DNA binding domain via dimerization.
“Intriguingly, the disordered linker is required to transduce the pH-dependent status of the periplasmic sensing domain to the DNA binding domain via dimerization.”
From Intrinsically disordered proteins play diverse roles in cell signaling (2022) · cites this paper as [161]
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- Authors
- Buchner, S., Schlundt, A., Lassak, J., Sattler, M., & Jung, K.
- Affiliations
- Center for Integrated Protein Science Munich (DE)
- Corresponding author
- Jung, Kirsten
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 2015-07
- Volume
- 427
- Issue
- 15
- Pages
- 2548-2561
- ISSN
- 0022-2836 (ISSN-L)
- OpenAlex
- W321250976
- Cited by
- 32
- References
- 47
- Citations by year
- 2026: 3 · 2025: 1 · 2024: 3 · 2023: 4 · 2022: 5 · 2021: 3 · 2020: 3 · 2019: 2 · 2018: 3 · 2017: 5
- FWCI
- 1.83
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Molecular Biology (publishedVersion)
- PubMed (publishedVersion)
- Site cant be reached (submittedVersion)
- PuSH - Publication Server of Helmholtz Zentrum München (submittedVersion)
- Funders
- Deutsche Forschungsgemeinschaft (Exc114/1, Exc114/2)
- Women Program of the Center for Integrated Protein Science Munich
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Endocrinology › Escherichia coli research studies
- Keywords
- CadC, pH sensing, intrinsically disordered regions, signal transduction, protein dimerization, DNA-binding domain, Escherichia coli
- MeSH terms
- Amino Acid Sequence, DNA, Bacterial, Escherichia coli, Hydrogen-Ion Concentration, Protein Binding, Structure-Activity Relationship, Signal Transduction, Trans-Activators, Protein Folding, Amino Acid Substitution, Escherichia coli Proteins, Protein Interaction Domains and Motifs, Protein Multimerization
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