Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Search research articles

Related Experiment Videos

The phage-shock-protein response.

Andrew J Darwin¹

¹Department of Microbiology, MSB 228, New York University School of Medicine, 550 First Avenue, New York, NY 10016, USA. darwia01@med.nyu.edu

Molecular Microbiology

|July 28, 2005

Summary

The phage-shock-protein (Psp) system protects bacteria from stress by maintaining cell energy and protein export. PspA is crucial for these functions, though other Psp proteins also play vital roles.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

Control of the <i>Pseudomonas aeruginosa</i> LbcA•CtpA proteolytic complex and its substrates.

Journal of bacteriology·2025

Same author

<i>In vivo</i> and <i>in vitro</i> analyses of the role of the Prc protease in inducing mucoidy in <i>Pseudomonas aeruginosa</i>.

Journal of bacteriology·2024

Same author

<i>In vivo</i> and <i>in vitro</i> analysis of the role of the Prc protease in inducing mucoidy in <i>Pseudomonas aeruginosa</i>.

bioRxiv : the preprint server for biology·2024

Same author

P. aeruginosa CtpA protease adopts a novel activation mechanism to initiate the proteolytic process.

The EMBO journal·2024

Same author

Correction for Wang et al., "An inhibitor/anti-inhibitor system controls the activity of lytic transglycosylase MltF in <i>Pseudomonas aeruginosa</i>".

mBio·2024

Same author

An inhibitor/anti-inhibitor system controls the activity of lytic transglycosylase MltF in <i>Pseudomonas aeruginosa</i>.

mBio·2023

Area of Science:

Bacteriology
Molecular Biology
Cellular Biology

Background:

The phage-shock-protein (Psp) system is a conserved bacterial response to extracytoplasmic stress.
This stress can compromise cellular energy status and is linked to various bacterial phenotypes.
Psp system mutants exhibit defects in proton-motive force, protein export, and survival under stress.

Purpose of the Study:

To summarize the current understanding of the bacterial Psp system.
To review inducing signals, signal transduction mechanisms, and physiological roles of the Psp system.
To present a genomic analysis of Psp system conservation across bacteria.

Main Methods:

Literature review and synthesis of existing research on the Psp system.
Analysis of phenotypes associated with Psp system mutations in various bacterial species (e.g., E. coli, Y. enterocolitica, S. enterica).
Genomic analysis to assess the conservation of Psp genes.

Main Results:

Psp system mutants show defects in proton-motive force maintenance, protein export (Sec and Tat pathways), alkaline pH survival, and biofilm formation.
Yersinia enterocolitica psp mutants exhibit growth defects and virulence issues when type III secretion systems are mislocalized.
PspA, a major component, is essential for most Psp-associated phenotypes, but not all, indicating roles for other Psp proteins.

Conclusions:

The Psp system is critical for bacterial adaptation to extracytoplasmic stress.
PspA likely acts as an effector, maintaining membrane integrity and proton-motive force.
Further research is needed to elucidate the roles of other Psp proteins, particularly in managing secretion system mislocalization.

Related Experiment Videos