1887

Abstract

Glycosylphosphatidyl inositol (GPI)-anchored proteins in are responsible for a vast range of functions, and deletions in certain GPI-anchored proteins severely reduce adhesion and virulence of this organism. In addition, completely modified GPIs are necessary for virulence. GPI anchor biosynthesis is essential for viability and starts with the transfer of -acetylglucosamine to phosphatidylinositol. This step is catalysed by a multi-subunit complex, GPI–-acetylglucosaminyltransferase (GPI–GnT). In this, the first report to our knowledge on a subunit of the GPI–GnT complex, we show that Gpi19p is the functional equivalent of the Gpi19p. An N-terminal truncation mutant of Gpi19p functionally complements a conditionally lethal mutant. Further, we constructed a conditional null mutant of by disrupting one allele and placing the remaining copy under the control of the MET3 promoter. Repression leads to growth defects, cell wall biogenesis aberrations, azole sensitivity and hyperfilamention. In addition, there is a noticeable gene dosage effect, with the heterozygote also displaying intermediate degrees of most phenotypes. The mutants also displayed a reduced susceptibility to the antifungal agent amphotericin B. Collectively, the results suggest that is required for normal morphology and cell wall architecture.

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2010-10-01
2024-04-23
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