Differential regulation of SAP8 and SAPS, which encode two new members of the secreted aspartic proteinase family in Candida albicans
- 1 October 1998
- journal article
- Published by Microbiology Society in Microbiology
- Vol. 144 (10), 2731-2737
- https://doi.org/10.1099/00221287-144-10-2731
Abstract
Secreted aspartic proteinases (Saps) contribute to the virulence of Candida albicans in systemic animal models of infection. Seven genes encoding Saps (SAP1-SAP7) have been identified to date but evidence suggested the existence of additional SAP genes. The screening of a C. albicans lambda EMBL3 genomic library for the presence of other SAP genes was undertaken. Two new genes, SAP8 and SAP9, were isolated. The N-terminal amino acid sequence deduced from SAP8 downstream of a Kex2p-like cleavage site corresponds to the N-terminal amino acid sequence of the 41 kDa Sap isolated and characterized previously. SAP8 mRNA was expressed preferentially in yeasts at 25 degrees C after 6 and 9 h growth in BSA-containing medium. SAP9 encodes an aspartic proteinase with a Kex2p-like cleavage site and contains a putative glycophosphatidylinositol-anchor signal at the C-terminus. Although the SAP9 gene product has not yet been isolated from cultures of C. albicans, transcripts of SAP9 were observed preferentially in later growth phases when SAP8 expression had decreased.Keywords
This publication has 20 references indexed in Scilit:
- The Yeast Proprotein Convertase Encoded by YAP3 Is a Glycophosphatidylinositol-anchored Protein That Localizes to the Plasma MembranePublished by Elsevier ,1995
- Expression of seven members of the gene family encoding secretory aspartyl proteinases in Candida albicansMolecular Microbiology, 1994
- Multiplicity of genes encoding secreted aspartic proteinases in Candida speciesMolecular Microbiology, 1994
- Transcription of the gene for a pepsinogen, PEP1, is regulated by white-opaque switching in Candida albicans.Molecular and Cellular Biology, 1992
- Elongation factor 3 (EF-3) from Candida albicans shows both structural and functional similarity to EF-3 from Saccharomyces cerevisiaeMolecular Microbiology, 1992
- A novel aspartyl protease allowing KEX2‐independent MFα propheromone processing in yeastYeast, 1990
- The pMTL nic− cloning vectors. I. Improved pUC polylinker regions to facilitate the use of sonicated DNA for nucleotide sequencingGene, 1988
- Minipreps of DNA from bacteriophage lambdaNucleic Acids Research, 1987
- A new method for predicting signal sequence cleavage sitesNucleic Acids Research, 1986
- Isolation of the putative structural gene for the lysine-arginine-cleaving endopeptidase required for processing of yeast prepro-α-factorCell, 1984