Evidence map›Paper›PMID 27279369›Full record

ArticleScientific reports2016

Contribution of the Twin Arginine Translocation system to the exoproteome of Pseudomonas aeruginosa.

Geneviève Ball, Haike Antelmann, Paul Roger Claude Imbert, Maxime Rémi Gimenez, Romé Voulhoux, Bérengère Ize

Abstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

19 citing papers in PubMed.

  1. Microbiology spectrum · 2026
    Article
  2. Microorganisms · 2026
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  3. Frontiers in microbiology · 2025
    Article
  4. Modelling host-pathogen interactions:Microbiology (Reading, England) · 2025
    Article
  5. Article
  6. Article
  7. ModifiedFrontiers in molecular biosciences · 2023
    Article
  8. Article
  9. Review
  10. Review
  11. Activity of a Synthetic Peptide Targeting MgtC onFrontiers in cellular and infection microbiology · 2019
    Article
  12. Article
  13. Article
  14. Two Rieske Fe/S Proteins and TAT System inFrontiers in plant science · 2018
    Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Tracking Proteins Secreted by Bacteria: What's in the Toolbox?Frontiers in cellular and infection microbiology · 2017
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors.

Geneviève BallLaboratoire d'Ingénierie des Systèmes Macromoléculaires (LISM-UMR7255) CNRS/Aix-Marseille Université, Institut de Microbiologie de la Méditerranée, Marseille, France.
Haike AntelmannInstitute for Biology-Microbiology, Freie Universität Berlin, Königin-Luise-Strasse 12-16, D-14195 Berlin, Germany.
Paul Roger Claude ImbertLaboratoire d'Ingénierie des Systèmes Macromoléculaires (LISM-UMR7255) CNRS/Aix-Marseille Université, Institut de Microbiologie de la Méditerranée, Marseille, France.
Maxime Rémi GimenezLaboratoire d'Ingénierie des Systèmes Macromoléculaires (LISM-UMR7255) CNRS/Aix-Marseille Université, Institut de Microbiologie de la Méditerranée, Marseille, France.
Romé VoulhouxLaboratoire d'Ingénierie des Systèmes Macromoléculaires (LISM-UMR7255) CNRS/Aix-Marseille Université, Institut de Microbiologie de la Méditerranée, Marseille, France.
Bérengère IzeLaboratoire d'Ingénierie des Systèmes Macromoléculaires (LISM-UMR7255) CNRS/Aix-Marseille Université, Institut de Microbiologie de la Méditerranée, Marseille, France.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

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.

Indexed as

Bacterial ProteinsPhosphatesProteomePseudomonas aeruginosaTwin-Arginine-Translocation SystemBacterial ProteinsPhosphatesProteomeTwin-Arginine-Translocation System

Identifiers

PMID27279369
PMCPMC4899797

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Registered trials

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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.