ArticleMolecular microbiology2009
Analysis of the Yersinia enterocolitica PspBC proteins defines functional domains, essential amino acids and new roles within the phage-shock-protein response.
Article in Molecular microbiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
18 citing papers in PubMed, 32 citations in OpenAlex.
- The phage shock protein (PSP) envelope stress response: discovery of novel partners and evolutionary history.mSystems · 2024Article
- Phyletic Distribution and Diversification of the Phage Shock Protein Stress Response System in Bacteria and Archaea.mSystems · 2022Article
- Contribution of YthA, a PspC Family Transcriptional Regulator of Lactococcus lactis F44 Acid Tolerance and Nisin Yield: a Transcriptomic Approach.Applied and environmental microbiology · 2018Article
- Article
- Interactions between the Cytoplasmic Domains of PspB and PspC Silence the Yersinia enterocolitica Phage Shock Protein Response.Journal of bacteriology · 2016Article
- 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
- Changes in Psp protein binding partners, localization and behaviour upon activation of the Yersinia enterocolitica phage shock protein response.Molecular microbiology · 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
- Links between type III secretion and extracytoplasmic stress responses in Yersinia.Frontiers in cellular and infection microbiology · 2012Review
- 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
- The evolution of the phage shock protein response system: interplay between protein function, genomic organization, and system function.Molecular biology and evolution · 2011Article
- Properties of the phage-shock-protein (Psp) regulatory complex that govern signal transduction and induction of the Psp response in Escherichia coli.Microbiology (Reading, England) · 2010Article
- Membrane association of PspA depends on activation of the phage-shock-protein response in Yersinia enterocolitica.Molecular microbiology · 2010Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The Yersinia enterocolitica phage-shock-protein (Psp) stress response system is activated by mislocalized outer-membrane secretin components of protein export systems and is essential for virulence. The cytoplasmic membrane proteins PspB and PspC were proposed to be dual function components of the system, acting both as positive regulators of psp gene expression and to support survival during secretin-induced stress. In this study we have uncoupled the regulatory and physiological functions of PspBC and discovered unexpected new roles, functional domains and essential amino acids. First, we showed that PspB controls PspC concentration by both pre- and post-transcriptional mechanisms. We then screened for PspBC mutants with altered transcriptional regulatory function. Unexpectedly, we identified PspB and PspC mutants that activated psp gene expression in the absence of secretin-induced stress. Together with a subsequent truncation analysis, this revealed that the PspC cytoplasmic domain plays an unforeseen role in negatively regulating psp gene expression. Conversely, mutations within the PspC periplasmic domain abolished its ability to activate psp gene expression. Significantly, PspC mutants unable to activate psp gene expression retained their ability to support survival during secretin-induced stress. These data provide compelling support for the proposal that these two functions are independent.
Indexed as
Identifiers
What OpenQuestion holds
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.