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.

Department of Membrane Transport Institute of Physiology AS CR v v i Videnska 1083 142 20 Prague 4 Krc Czech Republic

Citace poskytuje Crossref.org

The Candida albicans GAP gene family encodes permeases involved in general and specific amino acid uptake and sensing

Four pathogenic Candida species differ in salt tolerance

Chimeras between C. glabrata Cnh1 and S. cerevisiae Nha1 Na+/H+-antiporters are functional proteins increasing the salt tolerance of yeast cells

Functional comparison of plasma-membrane Na+/H+ antiporters from two pathogenic Candida species