Regeneration of the GTP-bound from the GDP-bound form of human and yeast ras proteins by nucleotide exchange. Stimulatory effect of organic and inorganic polyphosphates

The regeneration of the GTP-bound from the GDP-bound form of purified human and yeast ras proteins occurs in vitro by a nucleotide-exchange reaction. For both human and yeast ras proteins the dissociation of the protein-bound GDP is the rate-limiting step in the presence of Mg ions. The rate of formation of the ras X GTP complex is stimulated by weak Mg2+-chelating agents like ATP and inorganic polyphosphates and, to a lesser extent, by ADP. This suggests a possible mechanism of regulation of ras-dependent pathway(s) by intracellular metabolic products.