Plasma-membrane Cnh1 Na+/H+ antiporter regulates potassium homeostasis in Candida albicans
Language English Country England, Great Britain Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
- MeSH
- Anti-Bacterial Agents pharmacology MeSH
- Cell Membrane chemistry MeSH
- Candida albicans metabolism MeSH
- Cesium pharmacology MeSH
- Potassium Chloride pharmacology MeSH
- Lithium Chloride pharmacology MeSH
- Sodium Chloride pharmacology MeSH
- Chlorides pharmacology MeSH
- Gene Deletion MeSH
- Potassium metabolism MeSH
- Gene Expression MeSH
- Drug Resistance, Fungal MeSH
- Fungal Proteins analysis genetics metabolism MeSH
- Homeostasis MeSH
- Hyphae chemistry MeSH
- Cloning, Molecular MeSH
- Yeasts chemistry MeSH
- Sodium-Hydrogen Exchangers analysis genetics metabolism MeSH
- Rubidium pharmacology MeSH
- Saccharomyces cerevisiae genetics metabolism MeSH
- Substrate Specificity MeSH
- Genetic Complementation Test MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Anti-Bacterial Agents MeSH
- cesium chloride MeSH Browser
- Cesium MeSH
- Potassium Chloride MeSH
- Lithium Chloride MeSH
- Sodium Chloride MeSH
- Chlorides MeSH
- CNH1 protein, Candida albicans MeSH Browser
- Potassium MeSH
- Fungal Proteins MeSH
- Sodium-Hydrogen Exchangers MeSH
- rubidium chloride MeSH Browser
- Rubidium MeSH
The physiological role of Candida albicans Cnh1, a member of the Na+/H+ antiporter family, was characterized. Though CaCnh1p had broad substrate specificity and mediated efflux of at least four alkali metal cations upon heterologous expression in Saccharomyces cerevisiae, its presence in C. albicans cells was important especially for potassium homeostasis. In C. albicans, CaCnh1p tagged with GFP was localized in the plasma membrane of cells growing as both yeasts and hyphae. Deletion of CNH1 alleles did not affect tolerance to NaCl, LiCl or CsCl, but resulted in increased sensitivity to high external concentrations of KCl and RbCl. The potassium and rubidium tolerance of a cnh1 homozygous mutant was fully restored by reintegration of CNH1 into the genome. The higher sensitivity of the cnh1/cnh1 mutant to external KCl was caused by a lower K+ efflux from these cells. Together, the functional characterization of the CaCnh1 antiporter in C. albicans revealed that this antiporter plays a significant role in C. albicans physiology. It ensures potassium and rubidium tolerance and participates in the regulation of intracellular potassium content of C. albicans cells.
References provided by Crossref.org
Four pathogenic Candida species differ in salt tolerance
Functional comparison of plasma-membrane Na+/H+ antiporters from two pathogenic Candida species