Evidence map›Paper›PMID 23802570›Full record

ArticleMolecular microbiology2013

The mobility of two kinase domains in the Escherichia coli chemoreceptor array varies with signalling state.

Ariane Briegel, Peter Ames, James C Gumbart, Catherine M Oikonomou, John S Parkinson, Grant J Jensen

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 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing 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

50 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Bacterial chemoreceptor signaling complexes control kinase activity by stabilizing the catalytic domain of CheA.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  7. Recent structural advances in bacterial chemotaxis signalling.Current opinion in structural biology · 2023
    Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Studying bacterial chemosensory array with CryoEM.Biochemical Society transactions · 2021
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  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

6 authors.

Ariane BriegelCalifornia Institute of Technology, 1200 E. California Blvd, Pasadena, CA, 91125, USA.
Peter Ames
James C Gumbart
Catherine M Oikonomou
John S Parkinson
Grant J Jensen

Funding

UTAH REGIONAL CANCER CENTERP30CA042014 · NCI · UTAH STATE HIGHER EDUCATION SYSTEM--UNIVERSITY OF UTAH · PI Jared P Rutter · 1986 to 2026
$72.6M
Intracellular Signaling by Bacterial ChemoreceptorsR01GM019559 · NIGMS · UTAH STATE HIGHER EDUCATION SYSTEM--UNIVERSITY OF UTAH · PI JOHN S PARKINSON · 1985 to 2026
$12.3M
Structural Basis of ChemoreceptionR01GM101425 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI JENSEN, GRANT J · 2013 to 2016
$1.1M
INTRACELLULAR SIGNALING BY BACTERIAL CHEMORECEPTORSR37GM019559 · NIGMS · UNIVERSITY OF UTAH · PI PARKINSON, JOHN S · 1992 to 2001
$806k
Howard Hughes Medical InstituteNCI NIH HHS CA42014NCI NIH HHS P30 CA042014NIGMS NIH HHS GM101425NIGMS NIH HHS GM19559NIGMS NIH HHS R01 GM019559NIGMS NIH HHS R01 GM101425NIGMS NIH HHS R37 GM019559
6 · The paper itself

Abstract

Motile bacteria sense their physical and chemical environment through highly cooperative, ordered arrays of chemoreceptors. These signalling complexes phosphorylate a response regulator which in turn governs flagellar motor reversals, driving cells towards favourable environments. The structural changes that translate chemoeffector binding into the appropriate kinase output are not known. Here, we apply high-resolution electron cryotomography to visualize mutant chemoreceptor signalling arrays in well-defined kinase activity states. The arrays were well ordered in all signalling states, with no discernible differences in receptor conformation at 2-3 nm resolution. Differences were observed, however, in a keel-like density that we identify here as CheA kinase domains P1 and P2, the phosphorylation site domain and the binding domain for response regulator target proteins. Mutant receptor arrays with high kinase activities all exhibited small keels and high proteolysis susceptibility, indicative of mobile P1 and P2 domains. In contrast, arrays in kinase-off signalling states exhibited a range of keel sizes. These findings confirm that chemoreceptor arrays do not undergo large structural changes during signalling, and suggest instead that kinase activity is modulated at least in part by changes in the mobility of key domains.

Indexed as

Signal TransductionBacterial ProteinsCryoelectron MicroscopyElectron Microscope TomographyEscherichia coliEscherichia coli ProteinsHistidine KinaseMembrane ProteinsMethyl-Accepting Chemotaxis ProteinsModels, BiologicalModels, MolecularProtein ConformationBacterial ProteinscheA protein, E coliEscherichia coli ProteinsHistidine KinaseMembrane ProteinsMethyl-Accepting Chemotaxis Proteins

Identifiers

PMID23802570
PMCPMC3763515

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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.