Evidence map›Paper›PMID 24102920›Full record

ArticleMolecular microbiology2013

The putative Poc complex controls two distinct Pseudomonas aeruginosa polar motility mechanisms.

Kimberly N Cowles, Theresa S Moser, Albert Siryaporn, Natsai Nyakudarika, William Dixon, Jonathan J Turner, Zemer Gitai

Abstract read
In one paragraph

Article in Molecular microbiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Structure and Stoichiometry of the Ton Molecular Motor.International journal of molecular sciences · 2020
    Review
  6. The TonBJournal of bacteriology · 2019
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Type IV pilins regulate their own expression via direct intramembrane interactions with the sensor kinase PilS.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  15. Sensational biofilms: surface sensing in bacteria.Current opinion in microbiology · 2016
    Review
  16. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors.

Kimberly N CowlesDepartment of Molecular Biology, Princeton University, Princeton, NJ, 08544, USA.
Theresa S Moser
Albert Siryaporn
Natsai Nyakudarika
William Dixon
Jonathan J Turner
Zemer Gitai

Funding

Discovering Antibiotic Drugs & Targets via High-Throughput Bacterial Cell BiologyDP2OD004389 · OD · PRINCETON UNIVERSITY · PI GITAI, ZEMER · 2008 to 2008
$2.4M
Negative regulation of virulence in Pseudomonas aeruginosaF32AI095002 · NIAID · PRINCETON UNIVERSITY · PI SIRYAPORN, ALBERT · 2012 to 2014
$169k
Subcellular Protein Localization in Pseudomonas aeruginosa VirulenceF32AI074271 · NIAID · PRINCETON UNIVERSITY · PI COWLES, KIMBERLY N · 2008 to 2010
$149k
NIAID NIH HHS F32 AI074271NIAID NIH HHS F32AI074271NIAID NIH HHS F32 AI095002NIAID NIH HHS F32AI095002NIH HHS 1DP2OD004389-01NIH HHS DP2 OD004389
6 · The paper itself

Abstract

Each Pseudomonas aeruginosa cell localizes two types of motility structures, a single flagellum and one or two clusters of type IV pili, to the cell poles. Previous studies suggested that these motility structures arrive at the pole through distinct mechanisms. Here we performed a swimming motility screen to identify polar flagellum localization factors and discovered three genes homologous to the TonB/ExbB/ExbD complex that have defects in both flagella-mediated swimming and pilus-mediated twitching motility. We found that deletion of tonB3, PA2983 or PA2982 led to non-polar localization of the flagellum and FlhF, which was thought to sit at the top of the flagellar localization hierarchy. Surprisingly, these mutants also exhibited pronounced changes in pilus formation or localization, indicating that these proteins may co-ordinate both the pilus and flagellum motility systems. Thus, we have renamed PA2983 and PA2982, pocA and pocB, respectively, for polar organelle co-ordinator to reflect this function. Our results suggest that TonB3, PocA and PocB may form a membrane-associated complex, which we term the Poc complex. These proteins do not exhibit polar localization themselves, but are required for increased expression of pilus genes upon surface association, indicating that they regulate motility structures through either localization or transcriptional mechanisms.

Indexed as

Bacterial ProteinsFimbriae, BacterialFlagellaGene Expression Regulation, BacterialMembrane ProteinsMicroscopy, Electron, TransmissionMonomeric GTP-Binding ProteinsMovementPseudomonas aeruginosaSequence DeletionBacterial ProteinsflhF protein, BacteriaMembrane ProteinsMonomeric GTP-Binding ProteinstonB protein, Bacteria

Identifiers

PMID24102920
PMCPMC4666538

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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.