Acid Proteinase Secreted by Candida Tropicalis: Functional Analysis of Preproregion Cleavages in C. Tropicalis and Saccharomyces Cerevisiae Togni, Giuseppe and Sanglard, Dominique and Quadroni, Manfredo and Foundling, Stephen I. and Monod, Michel,, 142, 493-503 (1996), doi = https://doi.org/10.1099/13500872-142-3-493, publicationName = Microbiology Society, issn = 1350-0872, abstract= 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., language=, type=