Evidence map›Paper›PMID 21285349›Full record

ArticleThe Journal of biological chemistry2011

Mapping the interactions between Escherichia coli TolQ transmembrane segments.

Xiang Y-Z Zhang, Emilie L Goemaere, Nadir Seddiki, Hervé Célia, Marthe Gavioli, Eric Cascales, Roland Lloubes

Abstract read
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Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Tuning the stator subunit of the flagellar motor with coiled-coil engineering.Protein science : a publication of the Protein Society · 2023
    Article
  5. Hyperglycemia promotes myocardial dysfunction via the ERS-MAPK10 signaling pathway in db/db mice.Laboratory investigation; a journal of technical methods and pathology · 2022
    Article
  6. Article
  7. Review
  8. Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Microcompartments and protein machines in prokaryotes.Journal of molecular microbiology and biotechnology · 2013
    Review
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

7 authors.

Xiang Y-Z ZhangLaboratoire d'Ingénierie des Systèmes Macromoleculaires UPR9027, CNRS, Aix-Marseille Université, Marseille, France.
Emilie L Goemaere
Nadir Seddiki
Hervé Célia
Marthe Gavioli
Eric Cascales
Roland Lloubes

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The tolQRAB-pal operon is conserved in Gram-negative genomes. The TolQRA proteins of Escherichia coli form an inner membrane complex in which TolQR uses the proton-motive force to regulate TolA conformation and the in vivo interaction of TolA C-terminal region with the outer membrane Pal lipoprotein. The stoichiometry of the TolQ, TolR, and TolA has been estimated and suggests that 4-6 TolQ molecules are associated in the complex, thus involving interactions between the transmembrane helices (TMHs) of TolQ, TolR, and TolA. It has been proposed that an ion channel forms at the interface between two TolQ and one TolR TMHs involving the TolR-Asp(23), TolQ-Thr(145), and TolQ-Thr(178) residues. To define the organization of the three TMHs of TolQ, we constructed epitope-tagged versions of TolQ. Immunodetection of in vivo and in vitro chemically cross-linked TolQ proteins showed that TolQ exists as multimers in the complex. To understand how TolQ multimerizes, we initiated a cysteine-scanning study. Results of single and tandem cysteine substitution suggest a dynamic model of helix interactions in which the hairpin formed by the two last TMHs of TolQ change conformation, whereas the first TMH of TolQ forms intramolecular interactions.

Indexed as

Amino Acid SubstitutionCell MembraneEscherichia coliEscherichia coli ProteinsIon ChannelsMembrane ProteinsMultiprotein ComplexesMutation, MissensePeptide MappingProtein Structure, TertiaryEscherichia coli ProteinsIon ChannelsMembrane ProteinsMultiprotein ComplexestolA protein, E colitolQ protein, E colitolR protein, E coli

Identifiers

PMID21285349
PMCPMC3064227

What OpenQuestion holds

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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.