Three Candida albicans potassium uptake systems differ in their ability to provide Saccharomyces cerevisiae trk1trk2 mutants with necessary potassium
Jazyk angličtina Země Anglie, Velká Británie Médium print-electronic
Typ dokumentu časopisecké články
PubMed
27189364
DOI
10.1093/femsyr/fow039
PII: fow039
Knihovny.cz E-zdroje
- Klíčová slova
- Acu1 ATPase, Candida, Hak1 transporter, Trk1 transporter, cation homeostasis, potassium uptake,
- MeSH
- Candida albicans genetika metabolismus MeSH
- draslík metabolismus MeSH
- koncentrace vodíkových iontů MeSH
- kultivační média chemie MeSH
- membránové transportní proteiny genetika metabolismus MeSH
- proteiny přenášející kationty nedostatek MeSH
- rekombinantní proteiny genetika metabolismus MeSH
- Saccharomyces cerevisiae - proteiny MeSH
- Saccharomyces cerevisiae genetika růst a vývoj metabolismus MeSH
- testy genetické komplementace MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- draslík MeSH
- kultivační média MeSH
- membránové transportní proteiny MeSH
- proteiny přenášející kationty MeSH
- rekombinantní proteiny MeSH
- Saccharomyces cerevisiae - proteiny MeSH
- Trk1 protein, Candida albicans MeSH Prohlížeč
- TRK1 protein, S cerevisiae MeSH Prohlížeč
- TRK2 protein, S cerevisiae MeSH Prohlížeč
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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