| Title: | Saccharomyces cerevisiae STE14 gene is required for COOH-terminal methylation of a-factor mating pheromone |
| Author(s): | Marr RS; Blair LC; Thorner J; |
| Address: | "Department of Molecular and Cell Biology, University of California, Berkeley 94720" |
| ISSN/ISBN: | 0021-9258 (Print) 0021-9258 (Linking) |
| Abstract: | "Saccharomyces cerevisiae a-factor is a dodecapeptide pheromone in which the carboxyl group of the COOH-terminal cysteine residue is methyl-esterified and the sulfhydryl side chain is conjugated in thioether linkage to a farnesyl moiety. We found that MAT a ste14 mutant cells secreted a biologically inactive form of a-factor which had more hydrophilic character than the wild-type pheromone. The authentic pheromone could be metabolically labeled with [methyl-3H]methionine, and the resulting COOH-terminal methyl ester could be removed by mild alkaline hydrolysis. In contrast, a-factor secreted by ste14 mutants did not incorporate a base-labile 3H-methyl moiety. Base treatment converted the normal pheromone into a form which was biologically inactive and which comigrated with the ste14 form of the peptide upon thin-layer chromatography. These results indicate that STE14 gene function is required for COOH-terminal methylation of a-factor" |
| Keywords: | "DNA Transposable Elements Mating Factor Methionine/metabolism Methylation *Mutagenesis, Insertional *Peptide Biosynthesis *Peptides Pheromones/biosynthesis Saccharomyces cerevisiae/*genetics Sulfates/metabolism Sulfur Radioisotopes Tritium;" |
| Notes: | "MedlineMarr, R S Blair, L C Thorner, J eng CA09041/CA/NCI NIH HHS/ GM07232/GM/NIGMS NIH HHS/ GM21841/GM/NIGMS NIH HHS/ etc. Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. 1990/11/25 J Biol Chem. 1990 Nov 25; 265(33):20057-60" |
