Abstract
In eukaryotes small secreted peptides are often proteolytically cleaved from larger precursors. In Saccharomyces cerevisiae multiple proteolytic processing steps are required for production of mature 12-amino-acid a-factor from its 36-amino-acid precursor. This study provides additional genetic data supporting a direct role for Afc1p in cleavage of the carboxyl-terminal tripeptide from the CAAX motif of the prenylated a-factor precursor. In addition, Afc1p had a second role in a-factor processing that was independent of, and in addition to, its role in the carboxyl-terminal processing in vivo. Using ubiquitin-a-factor fusions we confirmed that the pro-region of the a-factor precursor was not required for production of the mature pheromone. However, the pro-region of the a-factor precursor contributed quantitatively to a-factor production.
MeSH Terms
Amino Acids/chemistry
Base Sequence
DNA Primers
Endopeptidases/metabolism
Mating Factor
Membrane Proteins
Metalloendopeptidases/metabolism
Peptides/metabolism
Proprotein Convertases
Protein Precursors/chemistry,metabolism
Protein Prenylation
Saccharomyces cerevisiae/metabolism
Saccharomyces cerevisiae Proteins
Substrate Specificity
Chemicals
Amino Acids
DNA Primers
Membrane Proteins
Peptides
Protein Precursors
Saccharomyces cerevisiae Proteins
Mating Factor
Endopeptidases
Proprotein Convertases
RCE1 protein, S cerevisiae
Metalloendopeptidases
STE24 protein, S cerevisiae
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Boyartchuk V L
Division of Genetics, Department of Molecular and Cell Biology, University of California, Berkeley, California 94720, USA.
Rine J
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