Evidence map›Paper›PMID 26713609›Full record

ArticleMolecular microbiology2016

Delineating PAS-HAMP interaction surfaces and signalling-associated changes in the aerotaxis receptor Aer.

Darysbel Garcia, Kylie J Watts, Mark S Johnson, Barry L Taylor

Open access · bronzeAbstract read
In one paragraph

Article in Molecular microbiology, 2016. 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
1.2field-weighted citation impact, top 21% 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

16 citing papers in PubMed, 24 citations in OpenAlex.

  1. Signaling mechanism of the transmembrane energy receptor Aer.bioRxiv : the preprint server for biology · 2026
    Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. PAS domains in bacterial signal transduction.Current opinion in microbiology · 2021
    Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. 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
  14. Article
  15. Article
  16. Identification of a Chemoreceptor inFrontiers in microbiology · 2016
    Article
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.

Darysbel GarciaDivision of Microbiology and Molecular Genetics, School of Medicine, Loma Linda University, Loma Linda, CA, 92350, USA.
Kylie J WattsDivision of Microbiology and Molecular Genetics, School of Medicine, Loma Linda University, Loma Linda, CA, 92350, USA.
Mark S JohnsonDivision of Microbiology and Molecular Genetics, School of Medicine, Loma Linda University, Loma Linda, CA, 92350, USA.
Barry L TaylorDivision of Microbiology and Molecular Genetics, School of Medicine, Loma Linda University, Loma Linda, CA, 92350, USA.
Loma Linda University · US

Funding

NIH-LLU Initiative for Maximizing Student DiversityR25GM060507 · NIGMS · LOMA LINDA UNIVERSITY · PI DE LEON, MARINO · 2001 to 2022
$11.3M
SENSORY TRANSDUCTION IN BACTERIAR01GM029481 · NIGMS · LOMA LINDA UNIVERSITY · PI TAYLOR, BARRY L · 1985 to 2011
$2.9M
NIGMS NIH HHS 2 R25 GM060507NIGMS NIH HHS R01 GM029481NIGMS NIH HHS R25 GM060507
6 · The paper itself

Abstract

The Escherichia coli aerotaxis receptor, Aer, monitors cellular oxygen and redox potential via FAD bound to a cytosolic PAS domain. Here, we show that Aer-PAS controls aerotaxis through direct, lateral interactions with a HAMP domain. This contrasts with most chemoreceptors where signals propagate along the protein backbone from an N-terminal sensor to HAMP. We mapped the interaction surfaces of the Aer PAS, HAMP and proximal signalling domains in the kinase-off state by probing the solvent accessibility of 129 cysteine substitutions. Inaccessible PAS-HAMP surfaces overlapped with a cluster of PAS kinase-on lesions and with cysteine substitutions that crosslinked the PAS β-scaffold to the HAMP AS-2 helix. A refined Aer PAS-HAMP interaction model is presented. Compared to the kinase-off state, the kinase-on state increased the accessibility of HAMP residues (apparently relaxing PAS-HAMP interactions), but decreased the accessibility of proximal signalling domain residues. These data are consistent with an alternating static-dynamic model in which oxidized Aer-PAS interacts directly with HAMP AS-2, enforcing a static HAMP domain that in turn promotes a dynamic proximal signalling domain, resulting in a kinase-off output. When PAS-FAD is reduced, PAS interaction with HAMP is relaxed and a dynamic HAMP and static proximal signalling domain convey a kinase-on output.

Indexed as

Protein Interaction Domains and MotifsSignal TransductionAmino AcidsBinding SitesCarrier ProteinsDisulfidesModels, MolecularProtein BindingProtein ConformationProtein MultimerizationAmino AcidsCarrier ProteinsDisulfides

Identifiers

PMID26713609
PMCPMC5156559
OpenAlexW2232298246

What OpenQuestion holds

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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.