Title: | Total in vitro maturation of the Saccharomyces cerevisiae a-factor lipopeptide mating pheromone |
Author(s): | Marcus S; Caldwell GA; Xue CB; Naider F; Becker JM; |
Address: | "Department of Microbiology, University of Tennessee, Knoxville 37996" |
Journal Title: | Biochem Biophys Res Commun |
DOI: | 10.1016/0006-291x(90)91592-g |
ISSN/ISBN: | 0006-291X (Print) 0006-291X (Linking) |
Abstract: | "The a-factor mating pheromone, produced by Saccharomyces cerevisiae a haploid cells, is post-translationally modified in a manner analogous to that of the ras proto-oncogene product. A consensus C-terminal amino acid sequence, -CAAX (C is cysteine, A is aliphatic amino acid, and X is any amino acid), is the target of these modifications, which include isoprenylation (essential for Ras function), proteolysis of the -AAX sequence, and carboxy methyl esterification. Recently, the RAM/DPR1 gene product was shown to be a component of the activity responsible for isoprenylation of both Ras and a-factor. In this report, we present an in vitro assay which not only detects a-factor isoprenylation, but also proteolysis and carboxy methyl esterification, and directly demonstrates, biochemically, the order of these processing events. This a-factor maturation assay may prove useful for screening agents which block any of the steps involved in the post-translational modification of the a-factor and Ras -CAAX sequences. Such agents would be potential anti-Ras-related cancer therapeutic drugs" |
Keywords: | "Amino Acid Sequence Antineoplastic Agents Base Sequence Consensus Sequence Mating Factor Methylation Molecular Sequence Data Mutation Peptides/*genetics Protein Processing, Post-Translational Proto-Oncogene Proteins/*genetics Saccharomyces cerevisiae/gene;" |
Notes: | "MedlineMarcus, S Caldwell, G A Xue, C B Naider, F Becker, J M eng GM-22086/GM/NIGMS NIH HHS/ GM-22087/GM/NIGMS NIH HHS/ Research Support, U.S. Gov't, P.H.S. 1990/11/15 Biochem Biophys Res Commun. 1990 Nov 15; 172(3):1310-6. doi: 10.1016/0006-291x(90)91592-g" |