Roles of prenyl protein proteases in maturation of Saccharomyces cerevisiae a-factor

Genetics. 1998 Sep;150(1):95-101. doi: 10.1093/genetics/150.1.95.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acids / chemistry
  • Base Sequence
  • DNA Primers
  • Endopeptidases / metabolism*
  • Mating Factor
  • Membrane Proteins*
  • Metalloendopeptidases / metabolism*
  • Peptides / metabolism*
  • Proprotein Convertases
  • Protein Precursors / chemistry
  • Protein Precursors / metabolism
  • Protein Prenylation*
  • Saccharomyces cerevisiae / metabolism*
  • Saccharomyces cerevisiae Proteins*
  • Substrate Specificity

Substances

  • 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