f Acid Proteinase Secreted by Candida Tropicalis: Functional Analysis of Preproregion Cleavages in C. Tropicalis and Saccharomyces Cerevisiae
- Authors: Giuseppe Togni, Dominique Sanglard, Manfredo Quadroni, Stephen I. Foundling, Michel Monod*M
- *Author for correspondence: M. Monod. Tel: +41 21 314 03 76. Fax: +41 21 314 03 78.
- Microbiology, March 1996 142: 493-503, doi: 10.1099/13500872-142-3-493
- Subject: Genetics And Molecular Biology
- Published Online:
The 40 kDa secreted aspartyl proteinase (Sapt1) of Candida tropicalis is a pepsin-like enzyme encoded by the SAPT1 gene. According to the deduced amino acid sequence, Sapt1 has a putative preproregion of 60 amino acids preceding the mature enzyme. Maturation and processing of Sapt1 was analysed in C. tropicalis and Saccharomyces cerevisiae strains expressing wild-type or mutated forms of SAPT1. In S. cerevisiae the glycosylated 46 kDa proenzyme was converted to the mature 40 kDa form of Sapt1 by KEX2-dependent proteolytic cleavage following the Lys59-Arg60 sequence. The replacement of Lys59-Arg60 by Lys59-Gly60 revealed that the precursor can be processed by an autocatalytic cleavage. This alternative processing pathway to produce mature Sapt1 is less efficient than the Kex2-mediated pathway. Finally, it was shown that in C. tropicalis and S. cerevisiae the removal of the proregion was a prerequisite for the secretion of Sapt1.
- Keyword(s): Saccharomyces cerevisiae, Candida tropicalis, secretion, Kex2 endopeptidase, secreted aspartyl proteinase
© Society for General Microbiology 1996 | Published by the Microbiology Society
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