| Title: | Hormone processing and membrane-bound proteinases in yeast |
| DOI: | 10.1002/j.1460-2075.1985.tb02333.x |
| ISSN/ISBN: | 0261-4189 (Print) 1460-2075 (Electronic) 0261-4189 (Linking) |
| Abstract: | "A search for maturating peptidases of the precursor protein of the mating hormone (pheromone) alpha-factor of Saccharomyces cerevisiae was performed using short model peptides representing those sequences of the precursor protein, where cleavage is thought to occur in vivo. This search was done in a mutant lacking several of the unspecific vacuolar peptidases. The chromogenic peptide Cbz-Tyr-Lys-Arg-4-nitroanilide led to the detection of a membrane-bound enzyme called proteinase yscF. Cleavage of the synthetic peptide derivative occurs after the basic amino acid pair, a proposed signal for hormone processing. Optimum pH for the reaction is 7.2. The enzyme does not cleave after single basic amino acid residues indicating that it is distinct from trypsin-like proteinases. Proteolytic activity is enhanced by Triton X-100. The enzyme is strongly inhibited by EGTA, EDTA and mercurials but insensitive to phenylmethylsulfonyl fluoride. The enzyme activity is strongly dependent on Ca2+ ions. In a mutant (kex2), which accumulates an over-glycosylated alpha-factor precursor, no proteinase yscF activity can be found. Membrane-bound peptidase activity possibly involved in removal of the arginyl and lysyl residues remaining at the carboxy terminus of the alpha-factor pheromone peptide after the initial cut of the precursor molecule could be identified by using the model peptides Cbz-Tyr-Lys-Arg and Cbz-Tyr-Lys" |
| Keywords: | Animals Carboxypeptidases/metabolism Endopeptidases/*metabolism Membranes/enzymology Oligopeptides/metabolism Pheromones/*metabolism Protein Precursors/metabolism Saccharomyces cerevisiae/*metabolism; |
| Notes: | "MedlineAchstetter, T Wolf, D H eng Research Support, Non-U.S. Gov't England 1985/01/01 EMBO J. 1985 Jan; 4(1):173-7. doi: 10.1002/j.1460-2075.1985.tb02333.x" |
