Evidence map›Paper›PMID 21803986›Full record

ArticleJournal of bacteriology2011

Mutational analysis of the control cable that mediates transmembrane signaling in the Escherichia coli serine chemoreceptor.

Smiljka Kitanovic, Peter Ames, John S Parkinson

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

29 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
  2. Article
  3. The structural logic of dynamic signaling in the Escherichia coli serine chemoreceptor.Protein science : a publication of the Protein Society · 2024
    Article
  4. The Structural Logic of Dynamic Signaling in thebioRxiv : the preprint server for biology · 2024
    Article
  5. Discovery of a New Chemoeffector forACS bio & med chem Au · 2022
    Article
  6. Article
  7. Article
  8. Article
  9. mBio · 2019
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. Article
  19. Bacterial chemoreceptor dynamics correlate with activity state and are coupled over long distances.Proceedings of the National Academy of Sciences of the United States of America · 2015
    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

3 authors at 1 institution in 1 country.

Smiljka KitanovicBiology Department, University of Utah, 257 South 1400 East, Salt Lake City, UT 84112, USA.
Peter Ames
John S Parkinson
University of Utah · US

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
INTRACELLULAR SIGNALING BY BACTERIAL CHEMORECEPTORSR37GM019559 · NIGMS · UNIVERSITY OF UTAH · PI PARKINSON, JOHN S · 1992 to 2001
$806k
NCI NIH HHS CA42014NCI NIH HHS P30 CA042014NIGMS NIH HHS GM19559NIGMS NIH HHS R01 GM019559NIGMS NIH HHS R37 GM019559
6 · The paper itself

Abstract

During transmembrane signaling by Escherichia coli Tsr, changes in ligand occupancy in the periplasmic serine-binding domain promote asymmetric motions in a four-helix transmembrane bundle. Piston displacements of the signaling TM2 helix in turn modulate the HAMP bundle on the cytoplasmic side of the membrane to control receptor output signals to the flagellar motors. A five-residue control cable joins TM2 to the HAMP AS1 helix and mediates conformational interactions between them. To explore control cable structural features important for signal transmission, we constructed and characterized all possible single amino acid replacements at the Tsr control cable residues. Only a few lesions abolished Tsr function, indicating that the chemical nature and size of the control cable side chains are not individually critical for signal control. Charged replacements at I214 mimicked the signaling consequences of attractant or repellent stimuli, most likely through aberrant structural interactions of the mutant side chains with the membrane interfacial environment. Prolines at residues 214 to 217 also caused signaling defects, suggesting that the control cable has helical character. However, proline did not disrupt function at G213, the first control cable residue, which might serve as a structural transition between the TM2 and AS1 helix registers. Hydrophobic amino acids at S217, the last control cable residue, produced attractant-mimic effects, most likely by contributing to packing interactions within the HAMP bundle. These results suggest a helix extension mechanism of Tsr transmembrane signaling in which TM2 piston motions influence HAMP stability by modulating the helicity of the control cable segment.

Indexed as

Bacterial ProteinsCell MembraneChemotaxisDNA Mutational AnalysisEscherichia coliMembrane ProteinsMethyl-Accepting Chemotaxis ProteinsModels, BiologicalProtein Structure, SecondaryProtein Structure, TertiarySignal TransductionBacterial ProteinsMembrane ProteinsMethyl-Accepting Chemotaxis Proteinstsr protein, E coli

Identifiers

PMID21803986
PMCPMC3187437
OpenAlexW2154941638

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.