Transport properties of a C. albicans amino-acid permease whose putative gene was cloned and expressed in S. cerevisiae
Jazyk angličtina Země Spojené státy americké Médium print
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
8299168
DOI
10.1007/bf00351710
Knihovny.cz E-zdroje
- MeSH
- aminokyseliny metabolismus MeSH
- biologický transport MeSH
- Candida albicans enzymologie genetika MeSH
- DNA fungální izolace a purifikace metabolismus MeSH
- exprese genu MeSH
- geny hub * MeSH
- kinetika MeSH
- klonování DNA MeSH
- membránové transportní proteiny genetika metabolismus MeSH
- restrikční mapování MeSH
- Saccharomyces cerevisiae metabolismus MeSH
- testy genetické komplementace MeSH
- transportní systémy aminokyselin MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- aminokyseliny MeSH
- DNA fungální MeSH
- membránové transportní proteiny MeSH
- transportní systémy aminokyselin 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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Properties of Candida albicans CAN1 permease expressed in Saccharomyces cerevisiae
