ArticleProceedings of the National Academy of Sciences of the United States of America2004
Alkalitolerance: a biological function for a multidrug transporter in pH homeostasis.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.
What it found
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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.
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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.
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Who cites it
65 citing papers in PubMed, 117 citations in OpenAlex.
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- The evolution of a NabioRxiv : the preprint server for biology · 2026Article
- Role of bacterial multidrug efflux pumps during infection.World journal of microbiology & biotechnology · 2024Review
- Article
- A genetic platform to investigate the functions of bacterial drug efflux pumps.Nature chemical biology · 2022Article
- Dissemination of ResistantFrontiers in microbiology · 2022Article
- Drug resistance: from bacteria to cancer.Molecular biomedicine · 2021Review
- Chemical or Genetic Alteration of Proton Motive Force Results in Loss of Virulence of Burkholderia glumae, the Cause of Rice Bacterial Panicle Blight.Applied and environmental microbiology · 2021Article
- The Whole Is Bigger than the Sum of Its Parts: Drug Transport in the Context of Two Membranes with Active Efflux.Chemical reviews · 2021Article
- Growth Response and Recovery ofFrontiers in microbiology · 2021Article
- The Evolutionary Conservation of Escherichia coli Drug Efflux Pumps Supports Physiological Functions.Journal of bacteriology · 2020Review
- Diverse Physiological Functions of Cation Proton Antiporters across Bacteria and Plant Cells.International journal of molecular sciences · 2020Review
- AFrontiers in microbiology · 2020Article
- Polar or Charged Residues Located in Four Highly Conserved Motifs Play a Vital Role in the Function or pH Response of a UPF0118 Family NaFrontiers in microbiology · 2020Article
- smFRET Probing Reveals Substrate-Dependent Conformational Dynamics of E. coli Multidrug MdfA.Biophysical journal · 2019Article
- Thermodynamic secrets of multidrug resistance: A new take on transport mechanisms of secondary active antiporters.Protein science : a publication of the Protein Society · 2018Review
- Biocide Selective TolC-Independent Efflux Pumps in Enterobacteriaceae.The Journal of membrane biology · 2018Article
- Characterization of a Functionally Unknown Arginine-Aspartate-Aspartate Family Protein FromFrontiers in microbiology · 2018Article
- Efflux drug transporters at the forefront of antimicrobial resistance.European biophysics journal : EBJ · 2017Review
5 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
MdfA is an Escherichia coli multidrug-resistance transporter. Cells expressing MdfA from a multicopy plasmid exhibit multidrug resistance against a diverse group of toxic compounds. In this article, we show that, in addition to its role in multidrug resistance, MdfA confers extreme alkaline pH resistance and allows the growth of transformed cells under conditions that are close to those used normally by alkaliphiles (up to pH 10) by maintaining a physiological internal pH. MdfA-deleted E. coli cells are sensitive even to mild alkaline conditions, and the wild-type phenotype is restored fully by MdfA expressed from a plasmid. This activity of MdfA requires Na(+) or K(+). Fluorescence studies with inverted membrane vesicles demonstrate that MdfA catalyzes Na(+)- or K(+)-dependent proton transport, and experiments with reconstituted proteoliposomes confirm that MdfA is solely responsible for this phenomenon. Studies with multidrug resistance-defective MdfA mutants and competitive transport assays suggest that these activities of MdfA are related. Together, the results demonstrate that a single protein has an unprecedented capacity to turn E. coli from an obligatory neutrophile into an alkalitolerant bacterium, and they suggest a previously uncharacterized physiological role for MdfA in pH homeostasis.
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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.