Title: | GPA1Val-50 mutation in the mating-factor signaling pathway in Saccharomyces cerevisiae |
Author(s): | Miyajima I; Arai K; Matsumoto K; |
Address: | "Department of Molecular Biology, DNAX Research Institute of Molecular and Cellular Biology, Palo Alto, California 94304" |
DOI: | 10.1128/mcb.9.6.2289-2297.1989 |
ISSN/ISBN: | 0270-7306 (Print) 1098-5549 (Electronic) 0270-7306 (Linking) |
Abstract: | "The GPA1 gene of Saccharomyces cerevisiae encodes a protein that is highly homologous to the alpha subunit of mammalian hetrotrimeric G proteins and is essential for haploid cell growth. A mutation of the GPA1 protein, GPA1Val-50, in which Gly-50 was replaced by valine, could complement the growth defect of a GPA1 disruption, gpal::HIS3. However, cells with gpa1::HIS3 expressing the GPA1Val-50 protein were supersensitive to alpha-factor in a short-term incubation but resumed growth after long-term incubation even after exposure to high concentrations of alpha-factor. The former phenotype associated with GPA1Val-50 is recessive, and the latter phenotype is dominant to GPA1+. The supersensitivity of GPA1Val-50 to alpha-factor was dependent on STE2 and STE4, which demonstrates that this GPA1Val-50-produced phenotype requires the mating-factor receptor and the beta subunit of the G protein. The double mutant of sst2-1 GPA1Val-50 recovered from division arrest, which suggested that SST2 is not required for recovery of the GPA1Val-50 mutant" |
Keywords: | "Amino Acid Sequence Cell Division GTP-Binding Proteins/*genetics/physiology *Genes, Fungal Genetic Complementation Test Glycine/*physiology Mating Factor Molecular Sequence Data Mutation Peptides/physiology Phenotype Plasmids Receptors, Cell Surface/physi;" |
Notes: | "MedlineMiyajima, I Arai, K Matsumoto, K eng 1989/06/01 Mol Cell Biol. 1989 Jun; 9(6):2289-97. doi: 10.1128/mcb.9.6.2289-2297.1989" |