Evidence map›Paper›PMID 23449919›Full record

ArticleMicrobiology (Reading, England)2013

The role of two Pseudomonas aeruginosa anthranilate synthases in tryptophan and quorum signal production.

Gregory C Palmer, Peter A Jorth, Marvin Whiteley

Open access · greenAbstract read
In one paragraph

Article in Microbiology (Reading, England), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
1.3field-weighted citation impact, top 19% of its field
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

31 citing papers in PubMed, 58 citations in OpenAlex.

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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

3 authors at 1 institution in 1 country.

Gregory C PalmerSection of Molecular Genetics and Microbiology, The Institute of Cell and Molecular Biology, The University of Texas at Austin, Austin, TX, USA.
Peter A JorthSection of Molecular Genetics and Microbiology, The Institute of Cell and Molecular Biology, The University of Texas at Austin, Austin, TX, USA.
Marvin WhiteleySection of Molecular Genetics and Microbiology, The Institute of Cell and Molecular Biology, The University of Texas at Austin, Austin, TX, USA.
The University of Texas at Austin · US

Funding

The molecular mechanisms of bacterial outer membrane vesicle formationR01AI075068 · NIAID · UNIVERSITY OF TEXAS AT AUSTIN · PI WHITELEY, MARVIN · 2007 to 2011
$1.8M
NIAID NIH HHS 5R01AI075068NIAID NIH HHS R01 AI075068
6 · The paper itself

Abstract

Pseudomonas aeruginosa is a Gram-negative, opportunistic pathogen that causes infections in the lungs of individuals with the genetic disease cystic fibrosis. Density-dependent production of toxic factors regulated by the Pseudomonas quinolone signal (2-heptyl-3-hydroxy-4-quinolone; PQS) have been proposed to be involved in P. aeruginosa virulence. PQS biosynthesis requires conversion of the central metabolite chorismate to anthranilate by anthranilate synthase. This reaction is also the first step in tryptophan biosynthesis. P. aeruginosa possesses two functional anthranilate synthases, TrpEG and PhnAB, and these enzymes are not functionally redundant, as trpEG mutants are tryptophan auxotrophs but produce PQS while mutants in phnAB are tryptophan prototrophs but do not produce PQS in minimal media. The goal of the work described in this paper was to determine the mechanism for this lack of functional complementation of TrpEG and PhnAB. Our results reveal that overexpression of either enzyme compensates for tryptophan auxotrophy and PQS production in the trpEG and phnAB mutants respectively, leading to the hypothesis that differential regulation of these genes is responsible for the lack of functional complementation. In support of this hypothesis, trpEG was shown to be expressed primarily during low-density growth while phnAB was expressed primarily at high density. Furthermore, dysregulation of phnAB expression eliminated tryptophan auxotrophy in the P. aeruginosa trpEG mutant. Based on these data, we propose a model for anthranilate sequestration by differential transcriptional regulation of the two P. aeruginosa anthranilate synthase enzymes.

Indexed as

Signal TransductionAnthranilate SynthaseBacterial ProteinsGene Expression Regulation, Bacterialortho-AminobenzoatesPhylogenyPseudomonas aeruginosaQuinolonesTryptophanAnthranilate Synthaseanthranilic acidBacterial Proteinsortho-AminobenzoatesQuinolonesTryptophan

Identifiers

PMID23449919
PMCPMC3709558
OpenAlexW2166445455

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.