Evidence map›Paper›PMID 11566988›Full record

ArticleJournal of bacteriology2001

GerN, an endospore germination protein of Bacillus cereus, is an Na(+)/H(+)-K(+) antiporter.

T W Southworth, A A Guffanti, A Moir, T A Krulwich

Abstract read
In one paragraph

Article in Journal of bacteriology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing 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

23 citing papers in PubMed.

  1. Article
  2. Atypical Serogroup IVb-v1 ofFrontiers in microbiology · 2022
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  15. Three two-component transporters with channel-like properties have monovalent cation/proton antiport activity.Proceedings of the National Academy of Sciences of the United States of America · 2007
    Article
  16. Article
  17. 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

4 authors.

T W SouthworthDepartment of Molecular Biology and Biotechnology, University of Sheffield, Sheffield S10 2TN, United Kingdom.
A A Guffanti
A Moir
T A Krulwich

Funding

PROTON COUPLING STRATEGIES IN ALKALIPHILIC BACILLUSR01GM028454 · NIGMS · MOUNT SINAI SCHOOL OF MEDICINE OF NYU · PI KRULWICH, TERRY ANN · 1985 to 2017
$6.2M
Tet Efflux Proteins: Implications of Multiple FunctionsR01GM052837 · NIGMS · MOUNT SINAI SCHOOL OF MEDICINE OF NYU · PI KRULWICH, TERRY ANN · 1996 to 2004
$1.2M
NIGMS NIH HHS GM28454NIGMS NIH HHS GM52837NIGMS NIH HHS R01 GM028454NIGMS NIH HHS R01 GM052837
6 · The paper itself

Abstract

GerN, a Bacillus cereus spore germination protein, exhibits homology to a widely distributed group of putative cation transporters or channel proteins. GerN complemented the Na(+)-sensitive phenotype of an Escherichia coli mutant that is deficient in Na(+)/H(+) antiport activity (strain KNabc). GerN also reduced the concentration of K(+) required to support growth of an E. coli mutant deficient in K(+) uptake (strain TK2420). In a fluorescence-based assay of everted E. coli KNabc membrane vesicles, GerN exhibited robust Na(+)/H(+) antiport activity, with a K(m) for Na(+) estimated at 1.5 mM at pH 8.0 and 25 mM at pH 7.0. Li(+), but not K(+), served as a substrate. GerN-mediated Na(+)/H(+) antiport was further demonstrated in everted vesicles as energy-dependent accumulation of (22)Na(+). GerN also used K(+) as a coupling ion without completely replacing H(+), as indicated by partial inhibition by K(+) of H(+) uptake into right-side-out vesicles loaded with Na(+). K(+) translocation as part of the antiport was supported by the stimulatory effect of intravesicular K(+) on (22)Na(+) uptake by everted vesicles and the dependence of GerN-mediated (86)Rb(+) efflux on the presence of Na(+) in trans. The inhibitory patterns of protonophore and thiocyanate were most consistent with an electrogenic Na(+)/H(+)-K(+) antiport. GerN-mediated Na(+)/H(+)-K(+) antiport was much more rapid than GerN-mediated Na(+)/H(+) antiport.

Indexed as

Bacterial ProteinsAntiportersBacillus cereusBiological Transport, ActiveCations, MonovalentCell PolarityEscherichia coliGenetic Complementation TestMembranesModels, BiologicalPotassiumRubidiumSodiumSodium-Hydrogen ExchangersSodium IsotopesSpores, BacterialAntiportersBacterial ProteinsCations, MonovalentGerN protein, Bacillus cereusPotassiumRubidiumSodiumSodium-Hydrogen ExchangersSodium Isotopes

Identifiers

PMID11566988
PMCPMC99667

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.