Differential activation of yeast adenylate cyclase by wild-type and mutant RAS proteins.
In these experiments we demonstrate that purified RAS proteins, whether derived from the yeast RAS1 or RAS2 or the human H-ras genes, activate yeast adenylate cyclase in the presence of guanine nucleotides. These results confirm the prediction of earlier genetic and biochemical data and for the first time provide a complete biochemical assay for RAS protein function. Furthermore, we observe a biochemical difference between the RAS2 and RAS2val19 proteins in their ability to activate adenylate cyclase after preincubation with GTP.
D000262:Adenylyl Cyclases / Q000378:metabolism*; D004789:Enzyme Activation / Q000187:drug effects; D005656:Fungal Proteins / Q000235:genetics / Q000302:isolation & purification / Q000494:pharmacology*; D006150:Guanine Nucleotides / Q000494:pharmacology; D006801:Humans; D008565:Membrane Proteins / Q000235:genetics / Q000302:isolation & purification / Q000494:pharmacology*; D009154:Mutation; D009857:Oncogenes; D012441:Saccharomyces cerevisiae / Q000201:enzymology / Q000235:genetics*; D029701:Saccharomyces cerevisiae Proteins; D018631:ras Proteins
D005656:Fungal Proteins; D006150:Guanine Nucleotides; D008565:Membrane Proteins; D029701:Saccharomyces cerevisiae Proteins; C489014:RAS1 protein, S cerevisiae; C489015:RAS2 protein, S cerevisiae; D018631:ras Proteins; D000262:Adenylyl Cyclases