| Title: | Isolation of the putative structural gene for the lysine-arginine-cleaving endopeptidase required for processing of yeast prepro-alpha-factor |
| Author(s): | Julius D; Brake A; Blair L; Kunisawa R; Thorner J; |
| DOI: | 10.1016/0092-8674(84)90442-2 |
| ISSN/ISBN: | 0092-8674 (Print) 0092-8674 (Linking) |
| Abstract: | "S. cerevisiae kex2 mutants are defective for the production of two biologically active secreted peptides: killer toxin and the mating pheromone, alpha-factor. Both molecules are excised from larger precursor polypeptides. In normal cells, the alpha-factor precursor is core-glycosylated and proteolytically processed intracellularly. In kex2 mutants, however, prepro-alpha-factor is not proteolytically cleaved and is secreted in a highly glycosylated form. All kex2 mutants examined (three independent alleles) lack a Zn++-sensitive membrane-associated endopeptidase with specificity for cleaving on the carboxyl side of a pair of basic residues. Absence of this activity cosegregates with the other phenotypes of a kex2 lesion in genetic crosses. The normal KEX2 gene was isolated by complementation of three of the phenotypes conferred by the kex2-1 mutation. The cloned DNA, either on a multicopy plasmid or integrated into the genome, restores both enzymatic activity in vitro and the normal pattern of proteolytic processing and glycosylation of prepro-alpha-factor in vivo. Gene dosage effects suggest that KEX2 is the structural gene for the endopeptidase" |
| Keywords: | "Arginine Genes Genes, Fungal Golgi Apparatus/metabolism Lysine Mating Factor Peptide Hydrolases/*genetics Peptides/*genetics *Protein Processing, Post-Translational Saccharomyces cerevisiae/enzymology/*genetics Substrate Specificity;" |
| Notes: | "MedlineJulius, D Brake, A Blair, L Kunisawa, R Thorner, J eng Research Support, U.S. Gov't, P.H.S. 1984/07/01 Cell. 1984 Jul; 37(3):1075-89. doi: 10.1016/0092-8674(84)90442-2" |
