Acid proteinase secreted by Candida tropicalis: functional analysis of preproregion cleavages in C. tropicalis and Saccharomyces cerevisiae.

Détails

ID Serval
serval:BIB_7B26651719CD
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Acid proteinase secreted by Candida tropicalis: functional analysis of preproregion cleavages in C. tropicalis and Saccharomyces cerevisiae.
Périodique
Microbiology
Auteur(s)
Togni G., Sanglard D., Quadroni M., Foundling S.I., Monod M.
ISSN
1350-0872[print], 1350-0872[linking]
Statut éditorial
Publié
Date de publication
1996
Volume
142 ( Pt 3)
Pages
493-503
Langue
anglais
Notes
Publication types: Journal Article
Publication Status: ppublish
Résumé
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.
Mots-clé
Candida/enzymology, Endopeptidases/genetics, Endopeptidases/metabolism, Enzyme Precursors/genetics, Enzyme Precursors/metabolism, Mutagenesis, Site-Directed, Plasmids/genetics, Saccharomyces cerevisiae/enzymology
Pubmed
Web of science
Open Access
Oui
Création de la notice
24/01/2008 16:46
Dernière modification de la notice
08/05/2019 20:48
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