Evidence map›Paper›PMID 27923921›Full record

ArticlemBio2016

High-Resolution pH Imaging of Living Bacterial Cells To Detect Local pH Differences.

Yusuke V Morimoto, Nobunori Kami-Ike, Tomoko Miyata, Akihiro Kawamoto, Takayuki Kato, Keiichi Namba, Tohru Minamino

Open access · goldAbstract read
In one paragraph

Article in mBio, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

32 citing papers in PubMed, 46 citations in OpenAlex.

  1. A β-cap on the FliPQR protein-export channel acts as the cap for initial flagellar rod assembly.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Frontiers of microbial movement research.Biophysics and physicobiology · 2023
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Membrane voltage-dependent activation mechanism of the bacterial flagellar protein export apparatus.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  15. The FlgN chaperone activates the NaCommunications biology · 2021
    Article
  16. Review
  17. Review
  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

7 authors at 1 institution in 1 country.

Yusuke V MorimotoGraduate School of Frontier Biosciences, Osaka University, Suita, Osaka, Japan.
Nobunori Kami-IkeGraduate School of Frontier Biosciences, Osaka University, Suita, Osaka, Japan.
Tomoko MiyataGraduate School of Frontier Biosciences, Osaka University, Suita, Osaka, Japan.
Akihiro KawamotoGraduate School of Frontier Biosciences, Osaka University, Suita, Osaka, Japan.
Takayuki KatoGraduate School of Frontier Biosciences, Osaka University, Suita, Osaka, Japan.
Keiichi NambaGraduate School of Frontier Biosciences, Osaka University, Suita, Osaka, Japan keiichi@fbs.osaka-u.ac.jp tohru@fbs.osaka-u.ac.jp.
Tohru MinaminoGraduate School of Frontier Biosciences, Osaka University, Suita, Osaka, Japan keiichi@fbs.osaka-u.ac.jp tohru@fbs.osaka-u.ac.jp.
Osaka University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protons are utilized for various biological activities such as energy transduction and cell signaling. For construction of the bacterial flagellum, a type III export apparatus utilizes ATP and proton motive force to drive flagellar protein export, but the energy transduction mechanism remains unclear. Here, we have developed a high-resolution pH imaging system to measure local pH differences within living Salmonella enterica cells, especially in close proximity to the cytoplasmic membrane and the export apparatus. The local pH near the membrane was ca. 0.2 pH unit higher than the bulk cytoplasmic pH. However, the local pH near the export apparatus was ca. 0.1 pH unit lower than that near the membrane. This drop of local pH depended on the activities of both transmembrane export components and FliI ATPase. We propose that the export apparatus acts as an H IMPORTANCE: The flagellar type III export apparatus is required for construction of the bacterial flagellum beyond the cellular membranes. The export apparatus consists of a transmembrane export gate and a cytoplasmic ATPase complex. The export apparatus utilizes ATP and proton motive force as the energy source for efficient and rapid protein export during flagellar assembly, but it remains unknown how. In this study, we have developed an in vivo pH imaging system with high spatial and pH resolutions with a pH indicator probe to measure local pH near the export apparatus. We provide direct evidence suggesting that ATP hydrolysis by the ATPase complex and the following rapid protein translocation by the export gate are both linked to efficient proton translocation through the gate.

Indexed as

Hydrogen-Ion ConcentrationOptical ImagingAntiportersCell MembraneCytoplasmSalmonella entericaSpatial AnalysisAntiporters

Identifiers

PMID27923921
PMCPMC5142619
OpenAlexW2560491362

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.