cDNA Cloning of an Aspartic Proteinase Secreted by Candida albicans
Open Access
- 14 November 1992
- journal article
- research article
- Published by Wiley in Microbiology and Immunology
- Vol. 36 (11) , 1207-1216
- https://doi.org/10.1111/j.1348-0421.1992.tb02124.x
Abstract
CDNA of an aspartic proteinase secreted by Candida albicans No. 114 was isolated using the polymerase chain reaction (PCR). The primary structure of the enzyme was deduced from the nucleotide sequence of the cDNA and compared with the structures of Saccharomyces cerevisiae proteinase A and vacuolar aspartyl proteinase of C. albicans. The mature aspartic proteinase consisted of 341 amino acid residues, and was 17.6 and 15.3% identical with the proteinase A and the aspartyl proteinase, respectively. Two active aspartic acid sites and the amino acids near those sites were conserved in the aspartic proteinase. We also showed that there is another gene of aspartic proteinase than that of strain ATCC10231 reported by Hube et al (J. Med. Vet. Mycol. 29 (1991)) in the same C. albicans genome, both in that strain and in No. 114.Keywords
This publication has 17 references indexed in Scilit:
- Codon utilisation in the pathogenic yeast,Candida albicansNucleic Acids Research, 1991
- Evidence That More Than One Gene Encodes n-Alkane-inducible Cytochrome P-450s in Candida maltosa, Found by Two-Step Gene Disruption.Agricultural and Biological Chemistry, 1991
- Nucleotide sequence of theCandida albicansaspartyl proteinase geneNucleic Acids Research, 1989
- Cloning and sequence analysis of cDNA for human cathepsin D.Proceedings of the National Academy of Sciences, 1985
- A putative signal peptidase recognition site and sequence in eukaryotic and prokaryotic signal peptidesJournal of Molecular Biology, 1983
- Determination of Nucleotide Sequences in DNAScience, 1981
- Properties of a purified proteinase from the yeast Candida albicansBiochimica et Biophysica Acta (BBA) - Enzymology, 1981
- Penicillopepsin from Penicillium janthinellum crystal structure at 2.8 Å and sequence homology with porcine pepsinNature, 1977
- Homology among acid proteases: comparison of crystal structures at 3A resolution of acid proteases from Rhizopus chinensis and Endothia parasitica.Proceedings of the National Academy of Sciences, 1977