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Envelope Stress Activates Expression of the Twin Arginine Translocation (Tat) System in Salmonella

The twin arginine translocation system (Tat) is a protein export system that is conserved in bacteria, archaea, and plants. In Gram-negative bacteria, it is required for the export of folded proteins from the cytoplasm to the periplasm. In Salmonella, there are 30 proteins that are predicted substra...

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Autores principales: Rogers, Alexandra R., Turner, Ezekeial E., Johnson, Deauna T., Ellermeier, Jeremy R.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Society for Microbiology 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9604234/
https://www.ncbi.nlm.nih.gov/pubmed/36036643
http://dx.doi.org/10.1128/spectrum.01621-22
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author Rogers, Alexandra R.
Turner, Ezekeial E.
Johnson, Deauna T.
Ellermeier, Jeremy R.
author_facet Rogers, Alexandra R.
Turner, Ezekeial E.
Johnson, Deauna T.
Ellermeier, Jeremy R.
author_sort Rogers, Alexandra R.
collection PubMed
description The twin arginine translocation system (Tat) is a protein export system that is conserved in bacteria, archaea, and plants. In Gram-negative bacteria, it is required for the export of folded proteins from the cytoplasm to the periplasm. In Salmonella, there are 30 proteins that are predicted substrates of Tat, and among these are enzymes required for anaerobic respiration and peptidoglycan remodeling. We have demonstrated that some conditions that induce bacterial envelope stress activate expression of a ΔtatABC-lacZ fusion in Salmonella enterica serovar Typhimurium. Particularly, the addition of bile salts to the growth medium causes a 3-fold induction of a ΔtatABC-lacZ reporter fusion. Our data demonstrate that this induction is mediated via the phage shock protein (Psp) stress response system protein PspA. Further, we show that deletion of tatABC increases the induction of tatABC expression in bile salts. Indeed, the data suggest significant interaction between PspA and the Tat system in the regulatory response to bile salts. Although we have not identified the precise mechanism of Psp regulation of tatABC, our work shows that PspA is involved in the activation of tatABC expression by bile salts and adds another layer of complexity to the Salmonella response to envelope stress. IMPORTANCE Salmonella species cause an array of diseases in a variety of hosts. This research is significant in showing induction of the Tat system as a defense against periplasmic stress. Understanding the underlying mechanism of this regulation broadens our understanding of the Salmonella stress response, which is critical to the ability of the organism to cause infection.
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spelling pubmed-96042342022-10-27 Envelope Stress Activates Expression of the Twin Arginine Translocation (Tat) System in Salmonella Rogers, Alexandra R. Turner, Ezekeial E. Johnson, Deauna T. Ellermeier, Jeremy R. Microbiol Spectr Research Article The twin arginine translocation system (Tat) is a protein export system that is conserved in bacteria, archaea, and plants. In Gram-negative bacteria, it is required for the export of folded proteins from the cytoplasm to the periplasm. In Salmonella, there are 30 proteins that are predicted substrates of Tat, and among these are enzymes required for anaerobic respiration and peptidoglycan remodeling. We have demonstrated that some conditions that induce bacterial envelope stress activate expression of a ΔtatABC-lacZ fusion in Salmonella enterica serovar Typhimurium. Particularly, the addition of bile salts to the growth medium causes a 3-fold induction of a ΔtatABC-lacZ reporter fusion. Our data demonstrate that this induction is mediated via the phage shock protein (Psp) stress response system protein PspA. Further, we show that deletion of tatABC increases the induction of tatABC expression in bile salts. Indeed, the data suggest significant interaction between PspA and the Tat system in the regulatory response to bile salts. Although we have not identified the precise mechanism of Psp regulation of tatABC, our work shows that PspA is involved in the activation of tatABC expression by bile salts and adds another layer of complexity to the Salmonella response to envelope stress. IMPORTANCE Salmonella species cause an array of diseases in a variety of hosts. This research is significant in showing induction of the Tat system as a defense against periplasmic stress. Understanding the underlying mechanism of this regulation broadens our understanding of the Salmonella stress response, which is critical to the ability of the organism to cause infection. American Society for Microbiology 2022-08-29 /pmc/articles/PMC9604234/ /pubmed/36036643 http://dx.doi.org/10.1128/spectrum.01621-22 Text en Copyright © 2022 Rogers et al. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution 4.0 International license (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Research Article
Rogers, Alexandra R.
Turner, Ezekeial E.
Johnson, Deauna T.
Ellermeier, Jeremy R.
Envelope Stress Activates Expression of the Twin Arginine Translocation (Tat) System in Salmonella
title Envelope Stress Activates Expression of the Twin Arginine Translocation (Tat) System in Salmonella
title_full Envelope Stress Activates Expression of the Twin Arginine Translocation (Tat) System in Salmonella
title_fullStr Envelope Stress Activates Expression of the Twin Arginine Translocation (Tat) System in Salmonella
title_full_unstemmed Envelope Stress Activates Expression of the Twin Arginine Translocation (Tat) System in Salmonella
title_short Envelope Stress Activates Expression of the Twin Arginine Translocation (Tat) System in Salmonella
title_sort envelope stress activates expression of the twin arginine translocation (tat) system in salmonella
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9604234/
https://www.ncbi.nlm.nih.gov/pubmed/36036643
http://dx.doi.org/10.1128/spectrum.01621-22
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