RAM, a gene of yeast required for a functional modification of RAS proteins and for production of mating pheromone a-factor.
We have identified a gene (SUPH) of S. cerevisiae that is required for both RAS function and mating by cells of a mating type. supH is allelic to ste16, a gene required for the production of the mating pheromone a-factor. Both RAS and a-factor coding sequences terminate with the potential acyltransferase recognition sequence Cys-A-A-X, where A is an aliphatic amino acid. Mutations in SUPH-STE16 prevent the membrane localization and maturation of RAS protein, as well as the fatty acid acylation of it and other membrane proteins. We propose the designation RAM (RAS protein and a-factor maturation function) for SUPH and STE16. RAM may encode an enzyme responsible for the modification and membrane localization of proteins with this C-terminal sequence.
D000215:Acylation; D000262:Adenylyl Cyclases / Q000378:metabolism; D000483:Alleles; D005656:Fungal Proteins / Q000235:genetics*; D005800:Genes, Fungal; D049770:Genes, Mating Type, Fungal; D000072235:Mating Factor; D008565:Membrane Proteins / Q000032:analysis / Q000235:genetics; D010452:Peptide Biosynthesis; D010455:Peptides / Q000235:genetics; D012441:Saccharomyces cerevisiae / Q000235:genetics*; D018631:ras Proteins
D005656:Fungal Proteins; D008565:Membrane Proteins; D010455:Peptides; D000072235:Mating Factor; D018631:ras Proteins; D000262:Adenylyl Cyclases