Evidence map›Paper›PMID 22210351›Full record

ArticleJournal of molecular biology2012

Energy complexes are apparently associated with the switch-motor complex of bacterial flagella.

Gabriel Zarbiv, Hui Li, Amnon Wolf, Gary Cecchini, S Roy Caplan, Victor Sourjik, Michael Eisenbach

Abstract read
In one paragraph

Article in Journal of molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.1field-weighted citation impact, top 25% 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

14 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Salmonella YqiC exerts its function through an oligomeric state.Protein science : a publication of the Protein Society · 2023
    Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Loose coupling in the bacterial flagellar motor.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. 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

7 authors at 3 institutions in 3 countries.

Gabriel ZarbivDepartment of Biological Chemistry, The Weizmann Institute of Science, 76100 Rehovot, Israel.
Hui Li
Amnon Wolf
Gary Cecchini
S Roy Caplan
Victor Sourjik
Michael Eisenbach
Weizmann Institute of Science · ILHeidelberg University · DEUniversity of California, San Francisco · US

Funding

Structure/Function of Complex ll OxidoreductasesR01GM061606 · NIGMS · NORTHERN CALIFORNIA INSTITUTE RES &EDUC · PI CECCHINI, GARY, IVERSON, T M · 2001 to 2022
$9.1M
NIGMS NIH HHS GM61606NIGMS NIH HHS R01 GM061606
6 · The paper itself

Abstract

Recently, the switch-motor complex of bacterial flagella was found to be associated with a number of non-flagellar proteins, which, in spite of not being known as belonging to the chemotaxis system, affect the function of the flagella. The observation that one of these proteins, fumarate reductase, is essentially involved in electron transport under anaerobic conditions raised the question of whether other energy-linked enzymes are associated with the switch-motor complex as well. Here, we identified two additional such enzymes in Escherichia coli. Employing fluorescence resonance energy transfer in vivo and pull-down assays invitro, we provided evidence for the interaction of F(0)F(1) ATP synthase via its β subunit with the flagellar switch protein FliG and for the interaction of NADH-ubiquinone oxidoreductase with FliG, FliM, and possibly FliN. Furthermore, we measured higher rates of ATP synthesis, ATP hydrolysis, and electron transport from NADH to oxygen in membrane areas adjacent to the flagellar motor than in other membrane areas. All these observations suggest the association of energy complexes with the flagellar switch-motor complex. Finding that deletion of the β subunit in vivo affected the direction of flagellar rotation and switching frequency further implied that the interaction of F(0)F(1) ATP synthase with FliG is important for the function of the switch of bacterial flagella.

Indexed as

Adenosine TriphosphateBacterial ProteinsElectron Transport Complex IEscherichia coliEscherichia coli ProteinsFluorescence Resonance Energy TransferGenes, SwitchHydrolysisModels, MolecularProton-Translocating ATPasesSuccinate DehydrogenaseAdenosine TriphosphateBacterial ProteinsElectron Transport Complex IEscherichia coli ProteinsFlig protein, BacteriaFliM protein, BacteriaFliN protein, BacteriaProton-Translocating ATPasesSuccinate Dehydrogenase

Identifiers

PMID22210351
PMCPMC4361073
OpenAlexW2061299493

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.