Autoactivation of proteinase A initiates activation of yeast vacuolar zymogens
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The Saccharomyces cerevisiae PEP4 gene encodes proteinase A, an aspartyl protease. pep4 mutants are defective in the activation of many vacuolar hydrolases, including proteinase B. We have expressed a pep4 mutation which directs the accumulation of pro-proteinase A with a defective active site. Co-expression with PEP4 leads to normal processing, i.e. the mutant zymogen is functional as a substrate for the maturation reaction in trans. We conclude that wild-type pro-proteinase A has the ability to mediate its own activation. Elimination of the co-expressed PEP4 gene did not effectively stop the processing of the mutant zymogen, owing to a strong, proteinase-B-dependent, phenotypic lag. In a proteinase-B-negative strain, processing of pro-proteinase A led to an active form of a higher molecular mass than the normal mature form.
Original language | English |
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Journal | European Journal of Biochemistry |
Volume | 207 |
Issue number | 1 |
Pages (from-to) | 277-83 |
Number of pages | 7 |
ISSN | 0014-2956 |
Publication status | Published - 1992 |
- Alleles, Amino Acid Sequence, Aspartic Acid Endopeptidases, Base Sequence, Binding Sites, Codon, Enzyme Activation, Enzyme Precursors, Genes, Fungal, Molecular Sequence Data, Mutagenesis, Site-Directed, Phenotype, Plasmids, Polymerase Chain Reaction, Protein Processing, Post-Translational, Restriction Mapping, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Vacuoles
Research areas
ID: 43974534