ArticleBiochemistry2010
The putative Na+/H+ antiporter of Vibrio cholerae, Vc-NhaP2, mediates the specific K+/H+ exchange in vivo.
Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 33 citations in OpenAlex.
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- Intestinal colonization againstAIMS microbiology · 2023Review
- Insights into the genome of Methylobacterium sp. NMS14P, a novel bacterium for growth promotion of maize, chili, and sugarcane.PloS one · 2023Article
- Genetic and Biochemical Characterization of the NaJournal of bacteriology · 2021Article
- Genomes of Gut Bacteria frommSystems · 2021Article
- Geochemical and metagenomics study of a metal-rich, green-turquoise-coloured stream in the southern Swiss Alps.PloS one · 2021Article
- Ion Binding and Selectivity of the NaThe journal of physical chemistry. B · 2020Article
- Role ofmSphere · 2020Article
- Physiological, Structural, and Functional Analysis of the Paralogous Cation-Proton Antiporters of NhaP Type fromInternational journal of molecular sciences · 2019Review
- Broad phylogenetic analysis of cation/proton antiporters reveals transport determinants.Nature communications · 2018Article
- Physiology of the Vc-NhaP paralogous group of cation-proton antiporters in Vibrio cholerae.Molecular and cellular biochemistry · 2017Article
- Alkaline Response of a Halotolerant Alkaliphilic Halomonas Strain and Functional Diversity of Its Na+(K+)/H+ Antiporters.The Journal of biological chemistry · 2016Article
- Effects of chromosomal deletion of the operon encoding the multiple resistance and pH-related antiporter in Vibrio cholerae.Microbiology (Reading, England) · 2016Article
- Growth Inhibition by External Potassium of Escherichia coli Lacking PtsN (EIIANtr) Is Caused by Potassium Limitation Mediated by YcgO.Journal of bacteriology · 2016Article
- Genetic Selection of Peptide Aptamers That Interact and Inhibit Both Small Protein B and Alternative Ribosome-Rescue Factor A of Aeromonas veronii C4.Frontiers in microbiology · 2016Article
- The C-terminal cytoplasmic portion of the NhaP2 cation-proton antiporter from Vibrio cholerae affects its activity and substrate affinity.Molecular and cellular biochemistry · 2014Article
- Na+/H+ antiport is essential for Yersinia pestis virulence.Infection and immunity · 2013Article
- Multidrug resistance protein MdtM adds to the repertoire of antiporters involved in alkaline pH homeostasis in Escherichia coli.BMC microbiology · 2013Article
- NhaP1 is a K+(Na+)/H+ antiporter required for growth and internal pH homeostasis of Vibrio cholerae at low extracellular pH.Microbiology (Reading, England) · 2012Article
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
The existence of bacterial K(+)/H(+) antiporters that prevent the overaccumulation of potassium in the cytoplasm was predicted by Peter Mitchell almost 50 years ago. The importance of K(+)/H(+) antiport for bacterial physiology is widely recognized, but its molecular mechanisms remain underinvestigated. Here, we demonstrate that a putative Na(+)/H(+) antiporter, Vc-NhaP2, protects cells of Vibrio cholerae growing at pH 6.0 from high concentrations of external K(+). Resistance of V. cholerae to Na(+) was found to be independent of Vc-NhaP2. When assayed in inside-out membrane vesicles derived from antiporter-deficient Escherichia coli, Vc-NhaP2 catalyzed the electroneutral K(+)(Rb(+))/H(+) exchange with a pH optimum of approximately 7.75 with an apparent K(m) for K(+) of 1.62 mM. In the absence of K(+), it exhibited Na(+)/H(+) antiport, albeit rather weakly. Interestingly, while Vc-NhaP2 cannot exchange Li(+) for protons, elimination of functional Vc-NhaP2 resulted in a significantly higher Li(+) resistance of V. cholerae cells growing at pH 6.0, suggesting the possibility of Vc-NhaP2-mediated Li(+)/K(+) antiport. The peculiar cation specificity of Vc-NhaP2 and the presence of its two additional paralogues in the same genome make this transporter an attractive model for detailed analysis of the structural determinants of the substrate specificity in alkali cation exchangers.
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