Degradation of Candida albicans Can1 permease expressed in Saccharomyces cerevisiae
Language English Country England, Great Britain Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
10418152
DOI
10.1111/j.1574-6968.1999.tb13670.x
PII: S0378-1097(99)00244-X
Knihovny.cz E-resources
- MeSH
- Candida albicans enzymology MeSH
- Time Factors MeSH
- Endocytosis MeSH
- Fungal Proteins * MeSH
- Genetic Vectors MeSH
- Ligases deficiency genetics MeSH
- Membrane Transport Proteins genetics metabolism MeSH
- Mutation MeSH
- Recombinant Proteins biosynthesis MeSH
- Saccharomyces cerevisiae genetics MeSH
- Amino Acid Transport Systems * MeSH
- Ubiquitin-Protein Ligases MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- CAN1 protein, Candida albicans MeSH Browser
- Fungal Proteins * MeSH
- Ligases MeSH
- Membrane Transport Proteins MeSH
- Recombinant Proteins MeSH
- Amino Acid Transport Systems * MeSH
- Ubiquitin-Protein Ligases MeSH
The Candida albicans amino-acid Can1 permease expressed in Saccharomyces cerevisiae is degraded in the vacuole after internalisation by endocytosis. The CaCan1 inactivation and degradation is slow and not inducible by ammonium ions or 'stress' conditions. Using Saccharomyces cerevisiae mutants defective in ubiquitin-protein ligase and ubiquitin-protein hydrolase we have shown that the degradation of heterologous CaCan1 permease is ubiquitin dependent.
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