Transport properties of a C. albicans amino-acid permease whose putative gene was cloned and expressed in S. cerevisiae
Language English Country United States Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
8299168
DOI
10.1007/bf00351710
Knihovny.cz E-resources
- MeSH
- Amino Acids metabolism MeSH
- Biological Transport MeSH
- Candida albicans enzymology genetics MeSH
- DNA, Fungal isolation & purification metabolism MeSH
- Gene Expression MeSH
- Genes, Fungal * MeSH
- Kinetics MeSH
- Cloning, Molecular MeSH
- Membrane Transport Proteins genetics metabolism MeSH
- Restriction Mapping MeSH
- Saccharomyces cerevisiae metabolism MeSH
- Genetic Complementation Test MeSH
- Amino Acid Transport Systems MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Amino Acids MeSH
- DNA, Fungal MeSH
- Membrane Transport Proteins MeSH
- Amino Acid Transport Systems MeSH
Using a gene bank of C. albicans, the lysine-permease deficiency in a strain of S. cerevisiae was complemented, and the restriction map of the corresponding C. albicans DNA fragment was constructed. Its expression in S. cerevisiae showed that the permease of C. albicans actively transports arginine (KT = 18 mumol/l, Jmax = 26 nmol/min per mg dry weight), lysine (KT = 12 mumol/l, Jmax = 18 nmol/min per mg dry weight), histidine (KT = 37 mumol/l, Jmax = 9.7 nmol/min per mg dry weight), as well as their toxic analogues canavanine and thialysine, with high affinity. The intracellular concentration of basic amino acids transported into S. cerevisiae by the C. albicans permease reaches more than a thousand-times-higher value compared to the external concentration in the medium. Accumulated amino acids do not leave the cells. The uptake is strongly reduced by the protonophores and inhibitors of plasma membrane H(+)-ATPase.
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