ArticleMicrobiology (Reading, England)2010
Properties of the phage-shock-protein (Psp) regulatory complex that govern signal transduction and induction of the Psp response in Escherichia coli.
Article in Microbiology (Reading, England), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 38 citations in OpenAlex.
- Engineered Phage Enables Efficient Control of Gene Expression upon Infection of the Host Cell.International journal of molecular sciences · 2024Article
- Comprehensive network of stress-induced responses in Zymomonas mobilis during bioethanol production: from physiological and molecular responses to the effects of system metabolic engineering.Microbial cell factories · 2024Review
- An Stomatin, Prohibitin, Flotillin, and HflK/C-Domain Protein Required to Link the Phage-Shock Protein to the Membrane inFrontiers in microbiology · 2021Article
- Proteogenomic Analysis ofFrontiers in microbiology · 2018Article
- Article
- Activity of a bacterial cell envelope stress response is controlled by the interaction of a protein binding domain with different partners.The Journal of biological chemistry · 2015Article
- A key hydrophobic patch identified in an AAA⁺ protein essential for its in trans inhibitory regulation.Journal of molecular biology · 2013Article
- Changes in Psp protein binding partners, localization and behaviour upon activation of the Yersinia enterocolitica phage shock protein response.Molecular microbiology · 2013Article
- Dynamics and stoichiometry of a regulated enhancer-binding protein in live Escherichia coli cells.Nature communications · 2013Article
- YjcC, a c-di-GMP phosphodiesterase protein, regulates the oxidative stress response and virulence of Klebsiella pneumoniae CG43.PloS one · 2013Article
- New functions for the ancient DedA membrane protein family.Journal of bacteriology · 2013Review
- Multiple envelope stress response pathways are activated in an Escherichia coli strain with mutations in two members of the DedA membrane protein family.Journal of bacteriology · 2013Article
- Phage shock protein C (PspC) of Yersinia enterocolitica is a polytopic membrane protein with implications for regulation of the Psp stress response.Journal of bacteriology · 2012Article
- The Tat system for membrane translocation of folded proteins recruits the membrane-stabilizing Psp machinery in Escherichia coli.The Journal of biological chemistry · 2012Article
- Phage shock proteins B and C prevent lethal cytoplasmic membrane permeability in Yersinia enterocolitica.Molecular microbiology · 2012Article
- Recent findings about the Yersinia enterocolitica phage shock protein response.Journal of microbiology (Seoul, Korea) · 2012Review
- Whole-genome sequencing and identification of Morganella morganii KT pathogenicity-related genes.BMC genomics · 2012Article
- FtsH-dependent degradation of phage shock protein C in Yersinia enterocolitica and Escherichia coli.Journal of bacteriology · 2011Article
- The Yersinia enterocolitica phage shock proteins B and C can form homodimers and heterodimers in vivo with the possibility of close association between multiple domains.Journal of bacteriology · 2011Article
- Dissipation of proton motive force is not sufficient to induce the phage shock protein response in Escherichia coli.Current microbiology · 2011Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The phage-shock-protein (Psp) response maintains the proton-motive force (pmf) under extracytoplasmic stress conditions that impair the inner membrane (IM) in bacterial cells. In Escherichia coli transcription of the pspABCDE and pspG genes requires activation of σ(54)-RNA polymerase by the enhancer-binding protein PspF. A regulatory network comprising PspF-A-C-B-ArcB controls psp expression. One key regulatory point is the negative control of PspF imposed by its binding to PspA. It has been proposed that under stress conditions, the IM-bound sensors PspB and PspC receive and transduce the signal(s) to PspA via protein-protein interactions, resulting in the release of the PspA-PspF inhibitory complex and the consequent induction of psp. In this work we demonstrate that PspB self-associates and interacts with PspC via putative IM regions. We present evidence suggesting that PspC has two topologies and that conserved residue G48 and the putative leucine zipper motif are determinants required for PspA interaction and signal transduction upon stress. We also establish that PspC directly interacts with the effector PspG, and show that PspG self-associates. These results are discussed in the context of formation and function of the Psp regulatory complex.
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