| Title: | Yeast alpha factor is processed from a larger precursor polypeptide: the essential role of a membrane-bound dipeptidyl aminopeptidase |
| Author(s): | Julius D; Blair L; Brake A; Sprague G; Thorner J; |
| DOI: | 10.1016/0092-8674(83)90070-3 |
| ISSN/ISBN: | 0092-8674 (Print) 0092-8674 (Linking) |
| Abstract: | "Alpha factor mating pheromone is a peptide of 13 amino acids secreted by Saccharomyces cerevisiae alpha cells. Nonmating ('sterile,' or ste) alpha-cell mutants bearing defects in the STE13 gene do not produce normal alpha factor, but release a collection of incompletely processed forms (alpha factor) that have a markedly reduced specific biological activity. The major alpha-factor peptides have the structures H2N-GluAlaGluAla-alpha factor and H2N-AspAlaGluAla-alpha factor. The ste13 mutants lack a membrane-bound heat-stable dipeptidyl aminopeptidase (DPAPase A) that specifically cleaves on the carboxyl side of repeating -X-Ala- sequences. Absence of DPAPase A and the other phenotypes of a ste13 lesion cosegregate in genetic crosses. The cloned STE13 gene on a plasmid causes yeast cells to overproduce DPAPase A severalfold. A different cloned DNA segment, which weakly suppresses the ste13 defects, causes overproduction of a heat-labile activity (DPAPase B) by about tenfold. Other experiments indicate that DPAPase A action may be rate-limiting for alpha-factor maturation in normal alpha cells" |
| Keywords: | "Amino Acids/analysis Cloning, Molecular DNA/metabolism Dipeptidyl-Peptidases and Tripeptidyl-Peptidases/*metabolism Endopeptidases/*metabolism Mating Factor Mutation *Peptide Biosynthesis Peptides/analysis Protein Precursors/*metabolism Saccharomyces cere;" |
| Notes: | "MedlineJulius, D Blair, L Brake, A Sprague, G Thorner, J eng Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. 1983/03/01 Cell. 1983 Mar; 32(3):839-52. doi: 10.1016/0092-8674(83)90070-3" |
