Evidence map›Paper›PMID 17293423›Full record

ArticleJournal of bacteriology2007

Catalytic properties of Staphylococcus aureus and Bacillus members of the secondary cation/proton antiporter-3 (Mrp) family are revealed by an optimized assay in an Escherichia coli host.

Talia H Swartz, Masahiro Ito, Takayuki Ohira, Shinsuke Natsui, David B Hicks, Terry A Krulwich

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.0field-weighted citation impact, top 12% 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

33 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
  2. International journal of systematic and evolutionary microbiology · 2025
    Article
  3. Review
  4. Lineage-specific evolution ofApplied and environmental microbiology · 2024
    Article
  5. Isolation and CsFrontiers in microbiology · 2023
    Article
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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 at 2 institutions in 2 countries.

Talia H SwartzDepartment of Pharmacology and Biological Chemistry, Box 1603, Mount Sinai School of Medicine, 1 Gustave L. Levy Place, New York, NY 10029, USA.
Masahiro Ito
Takayuki Ohira
Shinsuke Natsui
David B Hicks
Terry A Krulwich
Icahn School of Medicine at Mount Sinai · USToyo University · JP

Funding

PROTON COUPLING STRATEGIES IN ALKALIPHILIC BACILLUSR01GM028454 · NIGMS · MOUNT SINAI SCHOOL OF MEDICINE OF NYU · PI KRULWICH, TERRY ANN · 1985 to 2017
$6.2M
NIGMS NIH HHS GM28454NIGMS NIH HHS R01 GM028454
6 · The paper itself

Abstract

Monovalent cation proton antiporter-3 (Mrp) family antiporters are widely distributed and physiologically important in prokaryotes. Unlike other antiporters, they require six or seven hydrophobic gene products for full activity. Standard fluorescence-based assays of Mrp antiport in membrane vesicles from Escherichia coli transformants have not yielded strong enough signals for characterization of antiport kinetics. Here, an optimized assay protocol for vesicles of antiporter-deficient E. coli EP432 transformants produced higher levels of secondary Na(+)(Li(+))/H(+) antiport than previously reported. Assays were conducted on Mrps from alkaliphilic Bacillus pseudofirmus OF4 and Bacillus subtilis and the homologous antiporter of Staphylococcus aureus (Mnh), all of which exhibited Na(+)(Li(+))/H(+) antiport. A second paralogue of S. aureus (Mnh2) did not. K(+), Ca(2+), and Mg(2+) did not support significant antiport by any of the test antiporters. All three Na(+)(Li(+))/H(+) Mrp antiporters had alkaline pH optima and apparent K(m) values for Na(+) that are among the lowest reported for bacterial Na(+)/H(+) antiporters. Using a fluorescent probe of the transmembrane electrical potential (DeltaPsi), Mrp Na(+)/H(+) antiport was shown to be DeltaPsi consuming, from which it is inferred to be electrogenic. These assays also showed that membranes from E. coli EP432 expressing Mrp antiporters generated higher DeltaPsi levels than control membranes, as did membranes from E. coli EP432 expressing plasmid-borne NhaA, the well-characterized electrogenic E. coli antiporter. Assays of respiratory chain components in membranes from Mrp and control E. coli transformants led to a hypothesis explaining how activity of secondary, DeltaPsi-consuming antiporters can elicit increased capacity for DeltaPsi generation in a bacterial host.

Indexed as

PotentiometryBacillusBacterial ProteinsEscherichia coliHydrogenLithiumMembrane PotentialsMembranesSodiumSodium-Hydrogen ExchangersStaphylococcus aureusTransformation, GeneticBacterial ProteinsHydrogenLithiumSodiumSodium-Hydrogen Exchangers

Identifiers

PMID17293423
PMCPMC1855852
OpenAlexW2146546082

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.