ArticleThe Journal of biological chemistry2015
Activity of a bacterial cell envelope stress response is controlled by the interaction of a protein binding domain with different partners.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 20 citations in OpenAlex.
- Envelope Stress Activates Expression of the Twin Arginine Translocation (Tat) System in Salmonella.Microbiology spectrum · 2022Article
- The RyfA small RNA regulates oxidative and osmotic stress responses and virulence in uropathogenic Escherichia coli.PLoS pathogens · 2021Article
- Variations on a theme: evolution of the phage-shock-protein system in Actinobacteria.Antonie van Leeuwenhoek · 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
- Bacterial Stress Responses during Host Infection.Cell host & microbe · 2016Review
- Exogenous Fatty Acids Protect Enterococcus faecalis from Daptomycin-Induced Membrane Stress Independently of the Response Regulator LiaR.Applied and environmental microbiology · 2016Article
- Modulating Salmonella Typhimurium's Response to a Changing Environment through Bacterial Enhancer-Binding Proteins and the RpoN Regulon.Frontiers in molecular biosciences · 2016Review
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) system is a highly conserved cell envelope stress response required for virulence in Yersinia enterocolitica and Salmonella enterica. In non-inducing conditions the transcription factor PspF is inhibited by an interaction with PspA. In contrast, PspA associates with the cytoplasmic membrane proteins PspBC during inducing conditions. This has led to the proposal that PspBC exists in an OFF state, which cannot recruit PspA, or an ON state, which can. However, nothing was known about the difference between these two states. Here, we provide evidence that it is the C-terminal domain of Y. enterocolitica PspC (PspC(CT)) that interacts directly with PspA, both in vivo and in vitro. Site-specific photocross-linking revealed that this interaction occurred only during Psp-inducing conditions in vivo. Importantly, we have also discovered that PspC(CT) can interact with the C-terminal domain of PspB (PspC(CT)·PspB(CT)). However, the PspC(CT)·PspB(CT) and PspC(CT)·PspA interactions were mutually exclusive in vitro. Furthermore, in vivo, PspC(CT) contacted PspB(CT) in the OFF state, whereas it contacted PspA in the ON state. These findings provide the first description of the previously proposed PspBC OFF and ON states and reveal that the regulatory switch is centered on a PspC(CT) partner-switching mechanism.
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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.