Roles of prenyl protein proteases in maturation of Saccharomyces cerevisiae a-factor.
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.
Boyartchuk
V L
VL
Division of Genetics, Department of Molecular and Cell Biology, University of California, Berkeley, California 94720, USA.
Rine
J
J
D000596:Amino Acids / Q000737:chemistry; D001483:Base Sequence; D017931:DNA Primers; D010450:Endopeptidases / Q000378:metabolism*; D000072235:Mating Factor; D008565:Membrane Proteins; D008666:Metalloendopeptidases / Q000378:metabolism*; D010455:Peptides / Q000378:metabolism*; D043484:Proprotein Convertases; D011498:Protein Precursors / Q000737:chemistry / Q000378:metabolism; D017368:Protein Prenylation; D012441:Saccharomyces cerevisiae / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins; D013379:Substrate Specificity
D000596:Amino Acids; D017931:DNA Primers; D008565:Membrane Proteins; D010455:Peptides; D011498:Protein Precursors; D029701:Saccharomyces cerevisiae Proteins; D000072235:Mating Factor; D010450:Endopeptidases; D043484:Proprotein Convertases; C105193:RCE1 protein, S cerevisiae; D008666:Metalloendopeptidases; C491251:STE24 protein, S cerevisiae