1887

Abstract

Prenylation is a post-translational protein modification process that results in correct protein localization to membranes in the cell. It is mediated by at least three prenyltransferases (PTFs) in eukaryotic cells. The gene encodes the common α-subunit of two PTFs, farnesyltransferase (FTase) and geranylgeranyltransferase I (GGTase I). In this study, the gene of the prenylation pathway in the opportunistic pathogen was analysed. The heterozygote trisomy test was used to demonstrate that is essential to the viability of mRNA in the yeast and hyphae growth states was not detected by Northern blot analysis, but was detected by RT-PCR. Drugs that inhibit mammalian PTFs do not alter cell growth, but they do inhibit FTase and GGTase I activities in cell-free enzyme assays. The data from genetic studies and cell-free enzyme assays suggest that the drugs may not have access to the cytoplasm. The regulation of PTF subunits was also examined in a strain in which was under the control of a regulable promoter. Overall, this study demonstrated that is essential to , indicating that protein prenylation is an indispensable cellular process in this yeast.

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2003-01-01
2024-04-25
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