Deactivation of the E. coli pH Stress Sensor CadC by Cadaverine

Haneburger, Ina; Fritz, Georg; Jurkschat, Nicole; Tetsch, Larissa; Eichinger, A.; Skerra, Arne; Gerland, Ulrich; Jung, Kirsten

doi:10.1016/j.jmb.2012.08.023

Cited by 33 publications

(29 citation statements)

References 33 publications

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“…The cad module is a conditional pH stress response system (135,136). Induced by acidification, the sensor CadC, a one-component receptor, promotes the expression of cadAB.…”

Section: Variability Of the Ai Production Rate: The Hybrid Push-pull mentioning

confidence: 99%

Core Principles of Bacterial Autoinducer Systems

Hense

Schuster

2015

Microbiol Mol Biol Rev

164

156

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SUMMARY Autoinduction (AI), the response to self-produced chemical signals, is widespread in the bacterial world. This process controls vastly different target functions, such as luminescence, nutrient acquisition, and biofilm formation, in different ways and integrates additional environmental and physiological cues. This diversity raises questions about unifying principles that underlie all AI systems. Here, we suggest that such core principles exist. We argue that the general purpose of AI systems is the homeostatic control of costly cooperative behaviors, including, but not limited to, secreted public goods. First, costly behaviors require preassessment of their efficiency by cheaper AI signals, which we encapsulate in a hybrid “push-pull” model. The “push” factors cell density, diffusion, and spatial clustering determine when a behavior becomes effective. The relative importance of each factor depends on each species' individual ecological context and life history. In turn, “pull” factors, often stress cues that reduce the activation threshold, determine the cellular demand for the target behavior. Second, control is homeostatic because AI systems, either themselves or through accessory mechanisms, not only initiate but also maintain the efficiency of target behaviors. Third, AI-controlled behaviors, even seemingly noncooperative ones, are generally cooperative in nature, when interpreted in the appropriate ecological context. The escape of individual cells from biofilms, for example, may be viewed as an altruistic behavior that increases the fitness of the resident population by reducing starvation stress. The framework proposed here helps appropriately categorize AI-controlled behaviors and allows for a deeper understanding of their ecological and evolutionary functions.

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“…The cad module is a conditional pH stress response system (135,136). Induced by acidification, the sensor CadC, a one-component receptor, promotes the expression of cadAB.…”

Section: Variability Of the Ai Production Rate: The Hybrid Push-pull mentioning

confidence: 99%

Core Principles of Bacterial Autoinducer Systems

Hense

Schuster

2015

Microbiol Mol Biol Rev

164

156

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“…The central component of this system is the membrane-integrated pH sensor and transcriptional activator CadC, which regulates induction of the cadBA operon under low pH. CadC activity is also dependent on the presence of lysine (15), and this lysine-dependent activation of CadC requires the co-sensor LysP, a lysine-specific permease (16).…”

mentioning

confidence: 99%

A Sensory Complex Consisting of an ATP-binding Cassette Transporter and a Two-component Regulatory System Controls Bacitracin Resistance in Bacillus subtilis

Dintner¹,

Heermann²,

Fang³

et al. 2014

Journal of Biological Chemistry

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Background: BceS-like histidine kinases strictly require BceAB-like ABC transporters for sensing of peptide antibiotics. Results: BceAB of Bacillus subtilis interacted with BceS in vivo and in vitro and specifically bound the substrate peptide bacitracin. Conclusion: Complex formation with the ABC transporter affects the activity of the histidine kinase. Significance: Histidine kinase and ABC transporter form a sensory complex for the detection of peptide antibiotics.

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“…1b) [18–19], but the necessity for CadC dimerization had never been demonstrated directly. Indeed, even the presumed N in -C o ut type II topology had not been validated experimentally.…”

Section: Discussionmentioning

confidence: 99%

“…Recent studies of CadC, primarily in the laboratory of Kirsten Jung [14–18], have revealed the basic principles of CadC function. Because of its similarity to ToxR and related proteins, CadC is assumed to be a single-span Type II (N in -C out ) membrane protein.…”

Section: Introductionmentioning

confidence: 99%

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Topology, Dimerization, and Stability of the Single-Span Membrane Protein CadC

Lindner

White

2014

Journal of Molecular Biology

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Under acid stress, Escherichia coli induce expression of CadA (lysine decarboxylase) and CadB (lysine/cadaverine antiporter) in a lysine-rich environment. The ToxR-like transcriptional activator CadC controls expression of the cadBA operon. Using a novel Signal Peptidase I (SPase I) cleavage assay, we show that CadC is a Type II single-span membrane protein (MP) with a cytoplasmic DNA binding domain and a periplasmic sensor domain. We further show that, as long assumed, dimerization of the sensor domain is required for activating the cadBA operon. We prove this using a chimera in which the periplasmic domain of RodZ—a Type II MP involved in the maintenance of the rod shape of E. coli—replaces the CadC sensor domain. Because the RodZ periplasmic domain cannot dimerize, the chimera cannot activate the operon. However, replacement of the TM domain of the chimera with the glycophorin-A (GpA) TM domain causes intramembrane dimerization and consequently operon activation. Using a low-expression protocol that eliminates extraneous TM-helix dimerization signals arising from protein over-expression, we enhanced dramatically the dynamic range of the β-galactosidase assay for cadBA activation. Consequently, the strength of the intramembrane dimerization of the GpA domain could be compared quantitatively with the strength of the much stronger periplasmic dimerization of CadC. For the signal-peptidase assay, we inserted a SPase I cleavage site (AAA or AQA) at the periplasmic end of the TM helix. Cleavage occured with high efficiency for all TM and periplasmic domains tested, thus eliminating the need for the cumbersome spheroplast-proteinase K method for topology determinations.

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Deactivation of the E. coli pH Stress Sensor CadC by Cadaverine

Cited by 33 publications

References 33 publications

Core Principles of Bacterial Autoinducer Systems

Core Principles of Bacterial Autoinducer Systems

A Sensory Complex Consisting of an ATP-binding Cassette Transporter and a Two-component Regulatory System Controls Bacitracin Resistance in Bacillus subtilis

Topology, Dimerization, and Stability of the Single-Span Membrane Protein CadC

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