ArticleMolecular microbiology2012
Phage shock proteins B and C prevent lethal cytoplasmic membrane permeability in Yersinia enterocolitica.
Article in Molecular microbiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 43 citations in OpenAlex.
- Heat stress induces phage tolerance ineLife · 2025Article
- The promiscuous biotin ligase TurboID reveals the proxisome of the T3SS chaperone IpgC inmSphere · 2024Article
- The expression of virulence genes increases membrane permeability and sensitivity to envelope stress in Salmonella Typhimurium.PLoS biology · 2022Article
- Stress Resistance Development and Genome-Wide Transcriptional Response of Escherichia coli O157:H7 Adapted to Sublethal Thymol, Carvacrol, andApplied and environmental microbiology · 2018Article
- 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
- Environmental Regulation of Yersinia Pathophysiology.Frontiers in cellular and infection microbiology · 2016Review
- 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
- A Shigella flexneri virulence plasmid encoded factor controls production of outer membrane vesicles.G3 (Bethesda, Md.) · 2014Article
- Regulation of bacterial virulence gene expression by cell envelope stress responses.Virulence · 2014Review
- 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
- Promoter swapping unveils the role of the Citrobacter rodentium CTS1 type VI secretion system in interbacterial competition.Applied and environmental microbiology · 2013Article
- Stress relief during host infection: The phage shock protein response supports bacterial virulence in various ways.PLoS pathogens · 2013Review
- 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
- Links between type III secretion and extracytoplasmic stress responses in Yersinia.Frontiers in cellular and infection microbiology · 2012Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The bacterial phage shock protein (Psp) stress response system is activated by events affecting the cytoplasmic membrane. In response, Psp protein levels increase, including PspA, which has been implicated as the master effector of stress tolerance. Yersinia enterocolitica and related bacteria with a defective Psp system are highly sensitive to the mislocalization of pore-forming secretin proteins. However, why secretins are toxic to psp null strains, whereas some other Psp inducers are not, has not been explained. Furthermore, previous work has led to the confounding and disputable suggestion that PspA is not involved in mitigating secretin toxicity. Here we have established a correlation between the amount of secretin toxicity in a psp null strain and the extent of cytoplasmic membrane permeability to large molecules. This leads to a morphological change resembling cells undergoing plasmolysis. Furthermore, using novel strains with dis-regulated Psp proteins has allowed us to obtain unequivocal evidence that PspA is not required for secretin-stress tolerance. Together, our data suggest that the mechanism by which secretin multimers kill psp null cells is by causing a profound defect in the cytoplasmic membrane permeability barrier. This allows lethal molecular exchange with the environment, which the PspB and PspC proteins can prevent.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.