Abstract
Studies were performed to unravel the activation and maturation mechanism of vacuolar (lysosomal) proteinases in Saccharomyces cerevisiae. In vivo and in vitro studies show that proteinase yscA and proteinase yscB are involved in the activation and processing event of pro-carboxypeptidase yscY. Processing and activation of pro-carboxypeptidase yscY by proteinase yscA depends on an additional factor contained in the vacuolar fraction. Comparable activation can be mimicked by sodium polyphosphate. Optimum pH for processing by this proteinase yscA-triggered event is 5. The proteinase yscA-triggered maturation process of pro-carboxypeptidase yscY leads to an intermediate mol. wt form of the enzyme which is, however, fully active. Proteinase yscB transfers the intermediate mol. wt form of the original precursor to the apparently authentic, mature and active carboxypeptidase yscY. An activation and maturation scheme is devised.
MeSH Terms
Aspartic Acid Endopeptidases
Carboxypeptidases/genetics,metabolism
Cathepsin A
Endopeptidases/metabolism
Enzyme Activation
Kinetics
Lysosomes/enzymology
Mutation
Organoids/enzymology
Protein Processing, Post-Translational
Saccharomyces cerevisiae/enzymology,genetics
Saccharomyces cerevisiae Proteins
Serine Endopeptidases/metabolism
Vacuoles/enzymology
Chemicals
Saccharomyces cerevisiae Proteins
Carboxypeptidases
Endopeptidases
Cathepsin A
PRC1 protein, S cerevisiae
serine carboxypeptidase
Serine Endopeptidases
yeast proteinase B
aspartic proteinase A
PEP4 protein, S cerevisiae
Aspartic Acid Endopeptidases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Mechler B
Biochemisches Institut, Universität Freiburg, FRG.
Müller H
Wolf D H
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