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J. Biol. Chem., Vol. 262, Issue 36, 17278-17284, 12, 1987
JJ Correia, LT Baty and RC Williams Jr
The relationship between the concentration of Mg2+ and the binding of GDP
and GTP to tubulin dimers was investigated by measuring the displacement of
the nucleotide bound at the exchangeable site (E-site) by radiolabeled GDP
and GTP. A wide range of concentrations of GTP, GDP, and Mg2+ was explored.
In the near absence of Mg2+, the affinity of tubulin for GDP was found to
be much greater than its affinity for GTP. In the presence of 1.0 mM Mg2+,
however, its affinity for GDP was slightly less than for GTP. The results
could be quantitatively described in terms of a small number of reversible
equilibria. Equilibrium constants, pertaining to measurements at 0 degrees
C, in 0.1 M piperazine-N,N'-bis(2-ethanesulfonic acid), 0.2 mM
dithioerythritol, 2 mM EGTA, pH 6.9, were obtained by nonlinear least
squares fitting of the data. When the association constant of tubulin for
GDP uncomplexed with Mg2+ was taken to be 1.6 X 10(7) M-1, that for
uncomplexed GTP was found to be no larger than 1.4 x 10(4) M-1, at least
1100-fold smaller. The association constant of tubulin for the GDP.Mg2+
complex was found to be 2.5-2.7 x 10(7) M-1, while that for the GTP.Mg2+
complex is 6.4-9.0 x 10(7) M-1.
Mg2+ dependence of guanine nucleotide binding to tubulin
Department of Molecular Biology, Vanderbilt University, Nashville, Tennessee 37235.
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