Two aspartic proteinases secreted by the pathogenic yeast Candida parapsilosis differ in expression pattern and catalytic properties
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Olga Hrušková-Heidingsfeldová
Abstract
Secreted aspartic proteinases (Sap) play a role in the virulence of pathogenic Candida spp. Candida parapsilosis possesses three genes encoding these enzymes: SAPP1, SAPP2, and SAPP3. We analyzed the expression of the SAPP1 and SAPP2 genes and the production of Sapp1p and Sapp2p proteinases in the presence of different nitrogen sources. While the SAPP2 transcript was present under all of the conditions tested, expression of SAPP1 was induced only by the presence of exogenous protein as the sole nitrogen source. The concentration of Sapp1p in the medium upon induction was at least one order of magnitude higher than the concentration of Sapp2p in all media tested in this study. Enzymological characterization of purified Sapp1p and Sapp2p demonstrated that Sapp2p has a more restricted substrate specificity and significantly lower catalytic activity than Sapp1p. Homology models of Sapp1p and Sapp2p revealed structural motifs that may be responsible for the differences between these two enzymes. Our results indicate that C. parapsilosis secretes a low level of Sapp2p proteinase with narrow substrate specificity and low proteolytic activity under most conditions, while expression and secretion of a higher amount of catalytically efficient Sapp1p enzymes is triggered in the presence of exogenous protein serving as a nitrogen source.
©2009 by Walter de Gruyter Berlin New York
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Articles in the same Issue
- Review
- Glutathione dysregulation and the etiology and progression of human diseases
- Protein Structure and Function
- Interaction of the porcine reproductive and respiratory syndrome virus nucleocapsid protein with the inhibitor of MyoD family-a domain-containing protein
- Role of catalytic and non-catalytic subsite residues in ribonuclease activity of human eosinophil-derived neurotoxin
- Cell Biology and Signaling
- Expression and localization of atypical PKC isoforms in liver parenchymal cells
- Regulation of phosphoenolpyruvate carboxylase in PVYNTN-infected tobacco plants
- The influence of linoleic and linolenic acid on the activity and intracellular localisation of phospholipase D in COS-1 cells
- Proteolysis
- Two aspartic proteinases secreted by the pathogenic yeast Candida parapsilosis differ in expression pattern and catalytic properties
- The assembly and activation of kinin-forming systems on the surface of human U-937 macrophage-like cells
- Determination of three amino acids causing alteration of proteolytic activities of staphylococcal glutamyl endopeptidases
