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Eukaryotic Cell, August 2003, p. 746-755, Vol. 2, No. 4
1535-9778/03/$08.00+0 DOI: 10.1128/EC.2.4.746-755.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.
Dana A. Davis,
Ryan Subaran,
Michelle Kim, and Aaron P. Mitchell*
Department of Microbiology and Institute of Cancer Research, Columbia University, New York, New York 10032
Received 2 May 2003/ Accepted 27 May 2003
The Candida albicans cell wall participates in both growth and morphological transitions between yeast and hyphae. Our studies here focus on Dfg5p and Dcw1p, two similar proteins with features of glycosylphosphatidylinositol-linked cell surface proteins. Mutants lacking Dfg5p are defective in alkaline pH-induced hypha formation; mutants lacking Dcw1p have no detected hypha formation defect. Both homozygote-triplication tests and conditional expression strategies indicate that dfg5 and dcw1 mutations are synthetically lethal. Therefore, Dfg5p and Dcw1p share a function required for growth. Epitope-tagged Dfg5p, created through an insertional mutagenesis strategy, is found in cell membrane and cell wall extract fractions, and endoglycosidase H digestion shows that Dfg5p undergoes N-linked mannosylation. Surprisingly, Dfg5p is required for expression of the hypha-specific gene HWP1 in alkaline media. Because Dfg5p is a cell surface protein, it is poised to generate or transmit an external signal required for the program of hypha-specific gene expression.
Present address: Department of Pharmacological Sciences and Experimental Medicine, University of Camerino, Camerino, Italy 62032.
Present address: Department of Microbiology, University of Minnesota, Minneapolis, MN 55455.
Present address: Duke University Medical Center, Durham, NC 27710.
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