ArticlePloS one2014
Dynamic interaction between the CpxA sensor kinase and the periplasmic accessory protein CpxP mediates signal recognition in E. coli.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed.
- ThemBio · 2026Article
- Article
- Cpx-signalling innpj antimicrobials and resistance · 2024Article
- A multi-scale expression and regulation knowledge base for Escherichia coli.Nucleic acids research · 2023Article
- Physiological and Transcriptomic Analyses ofMicroorganisms · 2023Article
- Molecular insights into Escherichia coli Cpx envelope stress response activation by the sensor lipoprotein NlpE.Molecular microbiology · 2023Article
- Bacterial virulence regulation through soluble peptidoglycan fragments sensing and response: knowledge gaps and therapeutic potential.FEMS microbiology reviews · 2023Article
- Mycobacterial Regulatory Systems Involved in the Regulation of Gene Expression Under Respiration-Inhibitory Conditions.Journal of microbiology (Seoul, Korea) · 2023Review
- YihE is a novel binding partner of Rho and regulates Rho-dependent transcription termination in the Cpx stress response.iScience · 2022Article
- Roles of Two-Component Signal Transduction Systems in Shigella Virulence.Biomolecules · 2022Review
- Cpx-signalling facilitates Hms-dependent biofilm formation by Yersinia pseudotuberculosis.NPJ biofilms and microbiomes · 2022Article
- The CpxA/CpxR two-component system mediates regulation ofFrontiers in microbiology · 2022Article
- Comparative Transcriptome Analysis Reveals Regulatory Factors Involved inFrontiers in cellular and infection microbiology · 2022Article
- Chaperone-Mediated Stress Sensing in Mycobacterium tuberculosis Enables Fast Activation and Sustained Response.mSystems · 2021Article
- Endophytic Bacterial Communities ofFrontiers in microbiology · 2021Article
- Characterization of the TyrR Regulon in the Rhizobacterium Enterobacter ludwigii UW5 Reveals Overlap with the CpxR Envelope Stress Response.Journal of bacteriology · 2020Article
- Complex Response of the CpxAR Two-Component System to β-Lactams on Antibiotic Resistance and Envelope Homeostasis inAntimicrobial agents and chemotherapy · 2020Article
- Urinary tract infections: microbial pathogenesis, host-pathogen interactions and new treatment strategies.Nature reviews. Microbiology · 2020Review
- How bacteria recognise and respond to surface contact.FEMS microbiology reviews · 2020Review
- Role of Regulated Proteolysis in the Communication of Bacteria With the Environment.Frontiers in molecular biosciences · 2020Review
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Two-component systems, consisting of an inner membrane sensor kinase and a cytosolic response regulator, allow bacteria to respond to changes in the environment. Some two-component systems are additionally orchestrated by an accessory protein that integrates additional signals. It is assumed that spatial and temporal interaction between an accessory protein and a sensor kinase modifies the activity of a two-component system. However, for most accessory proteins located in the bacterial envelope the mechanistic details remain unclear. Here, we analyzed the interaction between the periplasmic accessory protein CpxP and the sensor kinase CpxA in Escherichia coli in dependency of three specific stimuli. The Cpx two-component system responds to envelope stress and plays a pivotal role for the quality control of multisubunit envelope structures, including type three secretion systems and pili of different pathogens. In unstressed cells, CpxP shuts off the Cpx response by a yet unknown mechanism. We show for the first time the physical interaction between CpxP and CpxA in unstressed cells using bacterial two-hybrid system and membrane-Strep-tagged protein interaction experiments. In addition, we demonstrate that a high salt concentration and the misfolded pilus subunit PapE displace CpxP from the sensor kinase CpxA in vivo. Overall, this study provides clear evidence that CpxP modulates the activity of the Cpx system by dynamic interaction with CpxA in response to specific stresses.
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