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Ferric reductase genes involved in high‐affinity iron uptake are differentially regulated in yeast and hyphae of Candida albicans
Author(s) -
Jeeves Rose E.,
Mason Robert P.,
Woodacre Alexandra,
Cashmore Annette M.
Publication year - 2011
Publication title -
yeast
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.923
H-Index - 102
eISSN - 1097-0061
pISSN - 0749-503X
DOI - 10.1002/yea.1892
Subject(s) - multicopper oxidase , candida albicans , ferrous , reductase , biology , yeast , ferric , biochemistry , fungal protein , hypha , microbiology and biotechnology , saccharomyces cerevisiae , enzyme , chemistry , laccase , organic chemistry
The pathogenic yeast Candida albicans possesses a reductive iron uptake system which is active in iron‐restricted conditions. The sequestration of iron by this mechanism initially requires the reduction of free iron to the soluble ferrous form, which is catalysed by ferric reductase proteins. Reduced iron is then taken up into the cell by a complex of a multicopper oxidase protein and an iron transport protein. Multicopper oxidase proteins require copper to function and so reductive iron and copper uptake are inextricably linked. It has previously been established that Fre10 is the major cell surface ferric reductase in C. albicans and that transcription of FRE10 is regulated in response to iron levels. We demonstrate here that Fre10 is also a cupric reductase and that Fre7 also makes a significant contribution to cell surface ferric and cupric reductase activity. It is also shown, for the first time, that transcription of FRE10 and FRE7 is lower in hyphae compared to yeast and that this leads to a corresponding decrease in cell surface ferric, but not cupric, reductase activity. This demonstrates that the regulation of two virulence determinants, the reductive iron uptake system and the morphological form of C. albicans , are linked. Copyright © 2011 John Wiley & Sons, Ltd.