Vacuolar hydrolases have been thoroughly characterized in Saccharomyces cerevisiae, but their homologues in the fungal pathogen Candida albicans have received less attention. The genes APR1 and CPY1 of C. albicans encode putative vacuolar aspartic proteinase and serine carboxypeptidase, respectively. We examined properties of apr1Δ and cpy1Δ mutants, showing that Cpy1p molecular species detected in cell lysates of apr1Δ and its parental strain did not differ in molar mass. Processing of Cpy1p precursor is apparently independent of Apr1p. This is in contrast to S. cerevisiae, where vacuolar aspartic proteinase Pep4p is known to participate in the activation of other vacuolar hydrolases including serine carboxypeptidase. We also found that both apr1Δ and cpy1Δ strains are able to form hyphae in nutrient-rich filamentation media. However, proline as a sole nitrogen source induced filamentation only in cpy1Δ and its parental strain, but not in apr1Δ. This indicates the importance of Apr1p for the morphological transition under nitrogen-limited conditions. Despite that, the ability of apr1Δ to kill murine macrophages was not reduced under the conditions tested.
- MeSH
- aspartátové proteasy genetika metabolismus MeSH
- Candida albicans enzymologie genetika růst a vývoj metabolismus MeSH
- dusík metabolismus MeSH
- fungální proteiny genetika metabolismus MeSH
- kandidóza mikrobiologie MeSH
- lidé MeSH
- makrofágy mikrobiologie MeSH
- myši MeSH
- vakuoly enzymologie genetika MeSH
- zvířata MeSH
- Check Tag
- lidé MeSH
- myši MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
Vacuoles play an important role in the physiology of pathogenic Candida spp. However, information on Candida albicans vacuolar enzymes, their properties, and regulation is scarce. Expression of the genes APR1 and CPY1 encoding vacuolar aspartic protease and serine carboxypeptidase, respectively, was analyzed using a clinical isolate of C. albicans. The transcription of both APR1 and CPY1 was upregulated in midexponential phase, together with increasing size of the vacuoles, when C. albicans was cultivated in yeast extract-peptone-dextrose agar at 30 °C. However, simultaneous upregulation of protein synthesis occurred only for Cpy1p. Analysis of APR1 and CPY1 expression under nitrogen-limited conditions revealed that the genes were regulated on both the transcriptional and translational levels and detectable amounts of Apr1p were synthesized only when C. albicans was grown in nitrogen-limited media.
- MeSH
- aspartátové proteasy genetika metabolismus MeSH
- Candida albicans enzymologie genetika růst a vývoj MeSH
- dusík metabolismus MeSH
- karboxypeptidasy genetika metabolismus MeSH
- kultivační média metabolismus MeSH
- regulace genové exprese u hub MeSH
- upregulace MeSH
- vakuoly enzymologie MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- MeSH
- autofagie MeSH
- buněčné struktury ultrastruktura MeSH
- cytoplazmatické struktury ultrastruktura MeSH
- elektronová mikroskopie MeSH
- Golgiho aparát ultrastruktura MeSH
- histocytochemie MeSH
- kur domácí MeSH
- kyselá fosfatasa MeSH
- leukocyty * cytologie metabolismus MeSH
- lyzozomy * enzymologie metabolismus MeSH
- multivezikulární tělíska * ultrastruktura MeSH
- statistika jako téma MeSH
- střevní sliznice ultrastruktura MeSH
- vakuoly enzymologie metabolismus ultrastruktura MeSH
