Three Candida albicans potassium uptake systems differ in their ability to provide Saccharomyces cerevisiae trk1trk2 mutants with necessary potassium
Language English Country England, Great Britain Media print-electronic
Document type Journal Article
PubMed
27189364
DOI
10.1093/femsyr/fow039
PII: fow039
Knihovny.cz E-resources
- Keywords
- Acu1 ATPase, Candida, Hak1 transporter, Trk1 transporter, cation homeostasis, potassium uptake,
- MeSH
- Candida albicans genetics metabolism MeSH
- Potassium metabolism MeSH
- Hydrogen-Ion Concentration MeSH
- Culture Media chemistry MeSH
- Membrane Transport Proteins genetics metabolism MeSH
- Cation Transport Proteins deficiency MeSH
- Recombinant Proteins genetics metabolism MeSH
- Saccharomyces cerevisiae Proteins MeSH
- Saccharomyces cerevisiae genetics growth & development metabolism MeSH
- Genetic Complementation Test MeSH
- Publication type
- Journal Article MeSH
- Names of Substances
- Potassium MeSH
- Culture Media MeSH
- Membrane Transport Proteins MeSH
- Cation Transport Proteins MeSH
- Recombinant Proteins MeSH
- Saccharomyces cerevisiae Proteins MeSH
- Trk1 protein, Candida albicans MeSH Browser
- TRK1 protein, S cerevisiae MeSH Browser
- TRK2 protein, S cerevisiae MeSH Browser
Yeasts usually have one or two high-affinity potassium transporters. Two complete and one interrupted gene encoding three types of putative potassium uptake system exist in Candida albicans SC5314. As high intracellular potassium is essential for many yeast cell functions, the existence of three transporters with differing transport mechanisms (Trk uniporter, Hak cation-proton symporter, Acu ATPase) may help pathogenic C. albicans cells to acquire the necessary potassium in various organs and tissues of the host. When expressed in Saccharomyces cerevisiae lacking their own potassium uptake systems, all three putative transporters were able to provide cells with the ability to grow with low amounts of potassium over a broad range of external pH. Only CaTrk1 was properly recognized and secreted to the plasma membrane. Nevertheless, even the small number of CaHak1 and mainly CaAcu1 molecules which reached the plasma membrane resulted in an improved growth of cells in low potassium concentrations, suggesting a high affinity and capacity of the transporters. A single-point mutation restored the complete CaACU1 gene, and the resulting protein not only provided cells with the necessary potassium but also improved their tolerance to toxic lithium. In contrast to its known homologues, CaAcu1 did not seem to transport sodium.
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