Evidence map›Paper›PMID 20545849›Full record

ArticleMolecular microbiology2010

Gain-of-function mutations cluster in distinct regions associated with the signalling pathway in the PAS domain of the aerotaxis receptor, Aer.

Asharie J Campbell, Kylie J Watts, Mark S Johnson, Barry L Taylor

Open access · bronzeAbstract read
In one paragraph

Article in Molecular microbiology, 2010. 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
1.9field-weighted citation impact, top 15% 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

19 citing papers in PubMed, 29 citations in OpenAlex.

  1. Signaling mechanism of the transmembrane energy receptor Aer.bioRxiv : the preprint server for biology · 2026
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  7. Signal transduction in photoreceptor histidine kinases.Protein science : a publication of the Protein Society · 2019
    Review
  8. A zipped-helix cap potentiates HAMP domain control of chemoreceptor signaling.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
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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

4 authors at 1 institution in 1 country.

Asharie J CampbellDivision of Microbiology and Molecular Genetics, Loma Linda University, Loma Linda, CA 92350, USA.
Kylie J Watts
Mark S Johnson
Barry L Taylor
Loma Linda University · US

Funding

SENSORY TRANSDUCTION IN BACTERIAR01GM029481 · NIGMS · LOMA LINDA UNIVERSITY · PI TAYLOR, BARRY L · 1985 to 2011
$2.9M
NIGMS NIH HHS GM29481NIGMS NIH HHS R01 GM029481
6 · The paper itself

Abstract

The Aer receptor monitors internal energy (redox) levels in Escherichia coli with an FAD-containing PAS domain. Here, we randomly mutagenized the region encoding residues 14-119 of the PAS domain and found 72 aerotaxis-defective mutants, 24 of which were gain-of-function, signal-on mutants. The mutations were mapped onto an Aer homology model based on the structure of the PAS-FAD domain in NifL from Azotobacter vinlandii. Signal-on lesions clustered in the FAD binding pocket, the beta-scaffolding and in the N-cap loop. We suggest that the signal-on lesions mimic the 'signal-on' state of the PAS domain, and therefore may be markers for the signal-in and signal-out regions of this domain. We propose that the reduction of FAD rearranges the FAD binding pocket in a way that repositions the beta-scaffolding and the N-cap loop. The resulting conformational changes are likely to be conveyed directly to the HAMP domain, and on to the kinase control module. In support of this hypothesis, we demonstrated disulphide band formation between cysteines substituted at residues N98C or I114C in the PAS beta-scaffold and residue Q248C in the HAMP AS-2 helix.

Indexed as

MutationSignal TransductionAmino Acid SequenceCarrier ProteinsEscherichia coliEscherichia coli ProteinsFlavin-Adenine DinucleotideIntercellular Signaling Peptides and ProteinsMolecular ConformationMolecular Sequence DataProtein BindingProtein Structure, SecondaryProtein Structure, TertiaryAer protein, E coliCarrier ProteinsEscherichia coli ProteinsFlavin-Adenine DinucleotideIntercellular Signaling Peptides and Proteins

Identifiers

PMID20545849
PMCPMC2916861
OpenAlexW2108224986

What OpenQuestion holds

Textmetadata
LicenceTDM
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.