Differential activation of yeast adenylate cyclase by wild-type and mutant RAS proteins

Cell. 1985 Jul;41(3):763-9. doi: 10.1016/s0092-8674(85)80057-x.

Abstract

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.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adenylyl Cyclases / metabolism*
  • Enzyme Activation / drug effects
  • Fungal Proteins / genetics
  • Fungal Proteins / isolation & purification
  • Fungal Proteins / pharmacology*
  • Guanine Nucleotides / pharmacology
  • Humans
  • Membrane Proteins / genetics
  • Membrane Proteins / isolation & purification
  • Membrane Proteins / pharmacology*
  • Mutation
  • Oncogenes*
  • Saccharomyces cerevisiae / enzymology
  • Saccharomyces cerevisiae / genetics*
  • Saccharomyces cerevisiae Proteins*
  • ras Proteins*

Substances

  • Fungal Proteins
  • Guanine Nucleotides
  • Membrane Proteins
  • Saccharomyces cerevisiae Proteins
  • RAS1 protein, S cerevisiae
  • RAS2 protein, S cerevisiae
  • ras Proteins
  • Adenylyl Cyclases