%0 Journal Article %A Togni, Giuseppe %A Sanglard, Dominique %A Quadroni, Manfredo %A Foundling, Stephen I. %A Monod, Michel %T Acid Proteinase Secreted by Candida Tropicalis: Functional Analysis of Preproregion Cleavages in C. Tropicalis and Saccharomyces Cerevisiae %D 1996 %J Microbiology, %V 142 %N 3 %P 493-503 %@ 1465-2080 %R https://doi.org/10.1099/13500872-142-3-493 %K Saccharomyces cerevisiae %K Candida tropicalis %K secreted aspartyl proteinase %K Kex2 endopeptidase %K secretion %I Microbiology Society, %X 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. %U https://www.microbiologyresearch.org/content/journal/micro/10.1099/13500872-142-3-493