Evidence map›Paper›PMID 21255112›Full record

ArticleMolecular microbiology2011

PAS/poly-HAMP signalling in Aer-2, a soluble haem-based sensor.

Kylie J Watts, Barry L Taylor, Mark S Johnson

Open access · bronzeAbstract read
In one paragraph

Article in Molecular microbiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
1.2field-weighted citation impact, top 23% 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

28 citing papers in PubMed, 48 citations in OpenAlex.

  1. Review
  2. Review
  3. AlphaFold2 captures the conformational landscape of the HAMP signaling domain.Protein science : a publication of the Protein Society · 2024
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. PAS domains in bacterial signal transduction.Current opinion in microbiology · 2021
    Review
  13. Microbiology and molecular biology reviews : MMBR · 2021
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Sensory Repertoire of Bacterial Chemoreceptors.Microbiology and molecular biology reviews : MMBR · 2017
    Review
  20. 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

3 authors at 1 institution in 1 country.

Kylie J WattsDivision of Microbiology and Molecular Genetics, Loma Linda University, Loma Linda, CA 92350, USA. kwatts@llu.edu
Barry L Taylor
Mark S Johnson
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
The role of imidazoline receptor in type-2 diabetesP20MD001632 · NIMHD · LOMA LINDA UNIVERSITY · PI DE LEON, DAISY D. · 2005 to 2009
$8.0M
Research Training/Education CoreP20MD006988 · NIMHD · LOMA LINDA UNIVERSITY · PI CASIANO, CARLOS A. · 2012 to 2016
$6.2M
SENSORY TRANSDUCTION IN BACTERIAR01GM029481 · NIGMS · LOMA LINDA UNIVERSITY · PI TAYLOR, BARRY L · 1985 to 2011
$2.9M
NIGMS NIH HHS GM029481NIGMS NIH HHS R01 GM029481NIGMS NIH HHS R25 GM060507NIMHD NIH HHS 5P20MD001632NIMHD NIH HHS P20 MD001632NIMHD NIH HHS P20 MD006988
6 · The paper itself

Abstract

Poly-HAMP domains are widespread in bacterial chemoreceptors, but previous studies have focused on receptors with single HAMP domains. The Pseudomonas aeruginosa chemoreceptor, Aer-2, has an unusual domain architecture consisting of a PAS-sensing domain sandwiched between three N-terminal and two C-terminal HAMP domains, followed by a conserved kinase control module. The structure of the N-terminal HAMP domains was recently solved, making Aer-2 the first protein with resolved poly-HAMP structure. The role of Aer-2 in P. aeruginosa is unclear, but here we show that Aer-2 can interact with the chemotaxis system of Escherichia coli to mediate repellent responses to oxygen, carbon monoxide and nitric oxide. Using this model system to investigate signalling and poly-HAMP function, we determined that the Aer-2 PAS domain binds penta-co-ordinated b-type haem and that reversible signalling requires four of the five HAMP domains. Deleting HAMP 2 and/or 3 resulted in a kinase-off phenotype, whereas deleting HAMP 4 and/or 5 resulted in a kinase-on phenotype. Overall, these data support a model in which ligand-bound Aer-2 PAS and HAMP 2 and 3 act together to relieve inhibition of the kinase control module by HAMP 4 and 5, resulting in the kinase-on state of the Aer-2 receptor.

Indexed as

Signal TransductionAdaptation, PhysiologicalAmino Acid SequenceBacterial ProteinsCarbon MonoxideChemotaxisEscherichia coliEscherichia coli ProteinsHemeMolecular Sequence DataNitric OxideOxygenProtein BindingProtein Structure, QuaternaryProtein Structure, SecondaryProtein Structure, TertiaryARR-2 protein, Pseudomonas aeruginosaBacterial ProteinsCarbon MonoxideEscherichia coli ProteinsHemeNitric OxideOxygen

Identifiers

PMID21255112
PMCPMC3078727
OpenAlexW1575959820

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.