ArticleMolecular microbiology2013
Changes in Psp protein binding partners, localization and behaviour upon activation of the Yersinia enterocolitica phage shock protein response.
Article in Molecular microbiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 40 citations in OpenAlex.
- The cyanobacterial ESCRT-III protein IM30 forms biomolecular condensates at physiologically relevant conditions.Biophysical journal · 2026Article
- The phage shock protein (PSP) envelope stress response: discovery of novel partners and evolutionary history.mSystems · 2024Article
- Biophysical and Computational Approaches to Unravel pH-Dependent Conformational Change of PspA Assist PspA-PspF Complex Formation in Yersinia enterocolitica.The protein journal · 2022Article
- Disbalancing Envelope Stress Responses as a Strategy for Sensitization ofFrontiers in microbiology · 2021Article
- Characterization of the Vibrio cholerae Phage Shock Protein Response.Journal of bacteriology · 2019Article
- Envelope stress responses: balancing damage repair and toxicity.Nature reviews. Microbiology · 2019Review
- Functional Implications of Multiple IM30 Oligomeric States.Frontiers in plant science · 2019Review
- Evidence for a second regulatory binding site on PspF that is occupied by the C-terminal domain of PspA.PloS one · 2018Article
- Article
- Interactions between the Cytoplasmic Domains of PspB and PspC Silence the Yersinia enterocolitica Phage Shock Protein Response.Journal of bacteriology · 2016Article
- Mechanism of Action and Resistance to Daptomycin in Staphylococcus aureus and Enterococci.Cold Spring Harbor perspectives in medicine · 2016Review
- VIPP1 Has a Disordered C-Terminal Tail Necessary for Protecting Photosynthetic Membranes against Stress.Plant physiology · 2016Article
- Mechanisms of drug resistance: daptomycin resistance.Annals of the New York Academy of Sciences · 2015Review
- The co-transcriptome of uropathogenic Escherichia coli-infected mouse macrophages reveals new insights into host-pathogen interactions.Cellular microbiology · 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
- Localisation and interactions of the Vipp1 protein in cyanobacteria.Molecular microbiology · 2014Article
- Inhibitors of SCF-Skp2/Cks1 E3 ligase block estrogen-induced growth stimulation and degradation of nuclear p27kip1: therapeutic potential for endometrial cancer.Endocrinology · 2013Article
- Super-resolution fluorescence microscopy of the cardiac connexome reveals plakophilin-2 inside the connexin43 plaque.Cardiovascular research · 2013Article
- Stress relief during host infection: The phage shock protein response supports bacterial virulence in various ways.PLoS pathogens · 2013Review
- Substrate-dependent assembly of the Tat translocase as observed in live Escherichia coli cells.PloS one · 2013Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
PspA, -B and -C regulate the bacterial phage shock protein stress response by controlling the PspF transcription factor. Here, we have developed complementary approaches to study the behaviour of these proteins at their endogenous levels in Yersinia enterocolitica. First, we observed GFP-tagged versions with an approach that resolves individual protein complexes in live cells. This revealed that PspA, -B and -C share common behaviours, including a striking contrast before and after induction. In uninduced cells, PspA, -B and -C were highly mobile and widely distributed. However, induction reduced mobility and the proteins became more organized. Combining mCherry- and GFP-tagged proteins also revealed that PspA colocalizes with PspB and PspC into large stationary foci, often located close to the pole of induced cells. In addition, co-immunoprecipitation assays provided the first direct evidence supporting the model that PspA switches binding partners from PspF to PspBC upon induction. Together, these data suggest that PspA, -B and -C do not stably interact and are highly mobile before induction, perhaps sampling the status of the membrane and each other. However, an inducing signal promotes PspABC complex formation and their relocation to discrete parts of the membrane, which might then be important for mitigating envelope stress.
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