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Characterization of glycerophosphodiester transport in the pathogenic yeast, Candida albicans
Author(s) -
Bishop Andrew C.,
Sun Tao,
Johnson Mitchell E.,
Vogt Jana Patton
Publication year - 2011
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.25.1_supplement.552.1
Phospholipase B‐mediated cleavage of glycerophospholipids produces both intracellular and extracellular glycerophosphodiesters. Saccharomyces cerevisiae and Candida albicans contain genes encoding phospholipases of this type. In S. cerevisiae , a single gene, ScGIT1 , encodes a permease responsible for transporting glycerophosphodiesters, such as glycerophosphoinositol (GroPIns) and glycerophosphocholine (GroPCho) across the cell membrane. In contrast, the C. albicans genome contains four ORFs with a high degree of homology to the ScGIT1. C. albicans transports GroPCho at a rate of roughly 10‐fold greater magnitude as compared to S. cerevisiae . In addition, C. albicans utilizes GroPIns and GroPCho as sole sources of phosphate at the physiologically relevant pH of 7.5. GroPIns transport, but not GroPCho transport is regulated by phosphate in C. albicans . Deletion of CaGIT1 (ORF 19.34) abolishes GroPIns transport activity and the ability to use GroPIns as a phosphate source, but does not affect GroPCho transport.

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