Open AccessMolecular cloning and functional characterisation of a glucose transporter, CaHGT1 , of Candida albicans
Author(s) -
Varma Archana,
Singh Brij Bhan,
Karnani Neerja,
LichtenbergFraté Hella,
Höfer Milan,
Magee B.B.,
Prasad Rajendra
Publication year - 2000
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2000.tb08866.x
Subject(s) - major facilitator superfamily , candida albicans , biology , biochemistry , kluyveromyces lactis , corpus albicans , saccharomyces cerevisiae , yeast , transporter , microbiology and biotechnology , gene
We have cloned the first glucose transporter CaHGT1 ( C andida a lbicans h igh‐affinity g lucose t ransporter) of a pathogenic yeast, Candida albicans . The DNA sequence (GenBank accession number Y16834) analysis revealed an ORF encoding a novel protein of 545 amino acids with a predicted molecular mass of 60.67 kDa. The putative protein with 12 transmembrane domains has 51% identity with Kluyveromyces lactis high‐affinity glucose transporter, HGT1 . The protein signatures which are conserved and distinctive of the sugar transporters belonging to the major facilitator superfamily (MFS) were also found in CaHgt1p. When heterologously expressed, the ORF functionally complemented a mutant strain of Saccharomyces cerevisiae RE700A which was deleted in seven hexose transporter genes and thus was unable to grow or transport glucose. The expression of CaHGT1 in C. albicans showed a transcript of 1.6 kb which was enhanced in response to the human steroid hormone progesterone. Interestingly, the transcript levels were also enhanced in the presence of drugs, e.g. cycloheximide, chloramphenicol and benomyl. The results suggest that CaHGT1 , which encodes a MFS protein, could be linked to the drug resistance phenomenon in C. albicans .