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J. Biol. Chem., Vol. 261, Issue 24, 10963-10965, Aug, 1986
A Hall and AJ Self
There is growing evidence that the protein products of the ras gene family,
p21ras, can couple growth factor receptors to intracellular second
messenger production and in particular to phosphoinositol lipid turnover.
So far, however, there has been no direct proof that the ras proteins
function as typical regulatory G proteins. We show here that the human
p21N-ras protein, isolated from an Escherichia coli expression system, can
exist as a stable GDP complex which exchanges very slowly with exogenous
GTP, the half-life of the p21N-ras X GDP complex being around 20 min.
However, in low Mg2+ (0.5 microM) the exchange rate is dramatically
increased and the half-life of the p21N- ras X GDP complex is less than 30
s. Furthermore, in low Mg2+, the relative binding affinity of the protein
for GTP as compared to GDP is increased 10-fold. The effect of low Mg2+ on
the exchange rate of both normal and oncogenic mutant p21ras molecules is
identical. We propose that removal of Mg2+ in vitro induces a similar
conformational change to stimulation in vivo. The properties described here
are consistent with a G protein-like activity for p21N-ras.
The effect of Mg2+ on the guanine nucleotide exchange rate of p21N-ras
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