Molecular and phenotypic analysis of mutations causing anionic phospholipid deficiency in closely related yeast species
Language English Country United States Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
- MeSH
- Biofilms MeSH
- Phenotype MeSH
- Phospholipids chemistry deficiency MeSH
- Fungal Proteins chemistry genetics metabolism MeSH
- Hydrophobic and Hydrophilic Interactions MeSH
- Yeasts chemistry classification genetics physiology MeSH
- Molecular Sequence Data MeSH
- Mutation * MeSH
- Amino Acid Sequence MeSH
- Sequence Alignment MeSH
- Transferases (Other Substituted Phosphate Groups) chemistry genetics metabolism MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase MeSH Browser
- Phospholipids MeSH
- Fungal Proteins MeSH
- Transferases (Other Substituted Phosphate Groups) MeSH
The pel1 mutation in Saccharomyces cerevisiae and the Cgpgs1Delta mutation in Candida glabrata result in deficiency of mitochondrial phosphatidylglycerolphosphate synthase and lack of two anionic phospholipids, phosphatidylglycerol and cardiolipin. DNA sequence analysis of the PCR-amplified pel1 mutant allele revealed that the pel1 mutation resulted from a single amino-acid substitution (Glu(463)Lys) in the C-terminal part of encoded enzyme. The CgPGS1 gene cloned in a centromeric pFL38 vector functionally complemented the pel1 mutation in S. cerevisiae. Likewise, the ScPGS1 gene cloned in pCgACU5 plasmid fully complemented the Cgpgs1Delta mutation in C. glabrata. This mutation increased the cell surface hydrophobicity and decreased biofilm formation. These results support a close evolutionary relatedness of S. cerevisiae and C. glabrata and point to the relationship between expression of virulence factors and anionic phospholipid deficiency in pathogenic C. glabrata.
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