ArticleMolecular microbiology2010
Membrane association of PspA depends on activation of the phage-shock-protein response in Yersinia enterocolitica.
Article in Molecular microbiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 44 citations in OpenAlex.
- Heat stress induces phage tolerance ineLife · 2025Article
- Mechanism for Vipp1 spiral formation, ring biogenesis, and membrane repair.Nature structural & molecular biology · 2025Article
- Biophysical and Computational Approaches to Unravel pH-Dependent Conformational Change of PspA Assist PspA-PspF Complex Formation in Yersinia enterocolitica.The protein journal · 2022Article
- Bacterial Vipp1 and PspA are members of the ancient ESCRT-III membrane-remodeling superfamily.Cell · 2021Article
- Characterization of the Vibrio cholerae Phage Shock Protein Response.Journal of bacteriology · 2019Article
- Disruption of the NlpD lipoprotein of the plague pathogen Yersinia pestis affects iron acquisition and the activity of the twin-arginine translocation system.PLoS neglected tropical diseases · 2019Article
- Evidence for a second regulatory binding site on PspF that is occupied by the C-terminal domain of PspA.PloS one · 2018Article
- Article
- Protecting from Envelope Stress: Variations on the Phage-Shock-Protein Theme.Trends in microbiology · 2017Review
- Interactions between the Cytoplasmic Domains of PspB and PspC Silence the Yersinia enterocolitica Phage Shock Protein Response.Journal of bacteriology · 2016Article
- Evaluating the role of phage-shock protein A in Burkholderia pseudomallei.Microbiology (Reading, England) · 2015Article
- Article
- Identification of YsaP, the Pilotin of the Yersinia enterocolitica Ysa Type III Secretion System.Journal of bacteriology · 2015Article
- 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
- Contributions of the σ(W) , σ(M) and σ(X) regulons to the lantibiotic resistome of Bacillus subtilis.Molecular microbiology · 2013Article
- Changes in Psp protein binding partners, localization and behaviour upon activation of the Yersinia enterocolitica phage shock protein response.Molecular microbiology · 2013Article
- Stress relief during host infection: The phage shock protein response supports bacterial virulence in various ways.PLoS pathogens · 2013Review
- Dynamics and stoichiometry of a regulated enhancer-binding protein in live Escherichia coli cells.Nature communications · 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
- Differential control of the rate of 5'-end-dependent mRNA degradation in Escherichia coli.Journal of bacteriology · 2012Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Regulation of the bacterial phage-shock-protein (Psp) system involves communication between integral (PspBC) and peripheral (PspA) cytoplasmic membrane proteins and a soluble transcriptional activator (PspF). In this study protein subcellular localization studies were used to distinguish between spatial models for this putative signal transduction pathway in Yersinia enterocolitica. In non-inducing conditions PspA and PspF were almost exclusively in the soluble fraction, consistent with them forming an inhibitory complex in the cytoplasm. However, upon induction PspA, but not PspF, mainly associated with the membrane fraction. This membrane association was dependent on PspBC but independent of increased PspA concentration. Analysis of psp null, overexpression and altered function mutants further supported a model where PspA is predominantly membrane associated only when the system is induced. Activation of the Psp system normally leads to a large increase in PspA concentration and we found that this provided a second mechanism for its membrane association, which did not require PspBC. These data suggest that basal PspFABC protein levels constitute a regulatory switch that moves some PspA to the membrane when an inducing trigger is encountered. Once this switch is activated PspA concentration increases, which might then allow it to directly contact the membrane for its physiological function.
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