Contribution of the Twin Arginine Translocation system to the exoproteome of Pseudomonas aeruginosa.
The opportunistic pathogen Pseudomonas aeruginosa uses secretion systems to deliver exoproteins into the environment. These exoproteins contribute to bacterial survival, adaptation, and virulence. The Twin arginine translocation (Tat) export system enables the export of folded proteins into the periplasm, some of which can then be further secreted outside the cell. However, the full range of proteins that are conveyed by Tat is unknown, despite the importance of Tat for the adaptability and full virulence of P. aeruginosa. In this work, we explored the P. aeruginosa Tat-dependent exoproteome under phosphate starvation by two-dimensional gel analysis. We identified the major secreted proteins and new Tat-dependent exoproteins. These exoproteins were further analyzed by a combination of in silico analysis, regulation studies, and protein localization. Altogether we reveal that the absence of the Tat system significantly affects the composition of the exoproteome by impairing protein export and affecting gene expression. Notably we discovered three new Tat exoproteins and one novel type II secretion substrate. Our data also allowed the identification of two new start codons highlighting the importance of protein annotation for subcellular predictions. The new exoproteins that we identify may play a significant role in P. aeruginosa pathogenesis, host interaction and niche adaptation.
Laboratoire d'Ingénierie des Systèmes Macromoléculaires (LISM-UMR7255) CNRS/Aix-Marseille Université, Institut de Microbiologie de la Méditerranée, Marseille, France.
Geneviève
G
Ball
Institute for Biology-Microbiology, Freie Universität Berlin, Königin-Luise-Strasse 12-16, D-14195 Berlin, Germany.
Haike
H
Antelmann
Laboratoire d'Ingénierie des Systèmes Macromoléculaires (LISM-UMR7255) CNRS/Aix-Marseille Université, Institut de Microbiologie de la Méditerranée, Marseille, France.
Paul Roger Claude
PR
Imbert
Laboratoire d'Ingénierie des Systèmes Macromoléculaires (LISM-UMR7255) CNRS/Aix-Marseille Université, Institut de Microbiologie de la Méditerranée, Marseille, France.
Maxime Rémi
MR
Gimenez
Laboratoire d'Ingénierie des Systèmes Macromoléculaires (LISM-UMR7255) CNRS/Aix-Marseille Université, Institut de Microbiologie de la Méditerranée, Marseille, France.
Romé
R
Voulhoux
Laboratoire d'Ingénierie des Systèmes Macromoléculaires (LISM-UMR7255) CNRS/Aix-Marseille Université, Institut de Microbiologie de la Méditerranée, Marseille, France.
Bérengère
B
Ize
D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D010710:Phosphates / Q000378:metabolism; D020543:Proteome / Q000235:genetics / Q000378:metabolism; D011550:Pseudomonas aeruginosa / Q000235:genetics / Q000378:metabolism*; D000069294:Twin-Arginine-Translocation System / Q000235:genetics / Q000378:metabolism*
D001426:Bacterial Proteins; D010710:Phosphates; D020543:Proteome; D000069294:Twin-Arginine-Translocation System