Title : Interaction of mammalian mitochondrial elongation factor EF-Tu with guanine nucleotides.

Pub. Date : 2000 Sep

PMID : 11045624






11 Functional Relationships(s)
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1 Equilibrium dialysis with [3H]GDP was used to measure the equilibrium dissociation constant of the EF-Tu(mt) x GDP complex (K(GDP) = 1.0 +/- 0.1 microM). Guanosine Diphosphate eukaryotic translation elongation factor 1 alpha 1 Homo sapiens
2 Equilibrium dialysis with [3H]GDP was used to measure the equilibrium dissociation constant of the EF-Tu(mt) x GDP complex (K(GDP) = 1.0 +/- 0.1 microM). Guanosine Diphosphate eukaryotic translation elongation factor 1 alpha 1 Homo sapiens
3 Equilibrium dialysis with [3H]GDP was used to measure the equilibrium dissociation constant of the EF-Tu(mt) x GDP complex (K(GDP) = 1.0 +/- 0.1 microM). Guanosine Diphosphate eukaryotic translation elongation factor 1 alpha 1 Homo sapiens
4 Competition of GTP with a fluorescent derivative of GDP (mantGDP) for binding to EF-Tu(mt) was used to measure the dissociation constant of the EF-Tu(mt) x GTP complex (K(GTP) = 18 +/- 9 microM). Guanosine Diphosphate eukaryotic translation elongation factor 1 alpha 1 Homo sapiens
5 Competition of GTP with a fluorescent derivative of GDP (mantGDP) for binding to EF-Tu(mt) was used to measure the dissociation constant of the EF-Tu(mt) x GTP complex (K(GTP) = 18 +/- 9 microM). Guanosine Diphosphate eukaryotic translation elongation factor 1 alpha 1 Homo sapiens
6 Both K(GDP) and K(GTP) for EF-Tu(mt) are quite different (about two orders of magnitude higher) than the dissociation constants of the corresponding complexes formed by Escherichia coli EF-Tu. Guanosine Diphosphate eukaryotic translation elongation factor 1 alpha 1 Homo sapiens
7 Both K(GDP) and K(GTP) for EF-Tu(mt) are quite different (about two orders of magnitude higher) than the dissociation constants of the corresponding complexes formed by Escherichia coli EF-Tu. Guanosine Diphosphate eukaryotic translation elongation factor 1 alpha 1 Homo sapiens
8 The forward and reverse rate constants for the association and dissociation of the EF-Tu(mt) x GDP complex were determined using the change in the fluorescence of mantGDP upon interaction with EF-Tu(mt). Guanosine Diphosphate eukaryotic translation elongation factor 1 alpha 1 Homo sapiens
9 The forward and reverse rate constants for the association and dissociation of the EF-Tu(mt) x GDP complex were determined using the change in the fluorescence of mantGDP upon interaction with EF-Tu(mt). Guanosine Diphosphate eukaryotic translation elongation factor 1 alpha 1 Homo sapiens
10 These values are in agreement with a simple equilibrium binding interaction between EF-Tu(mt) and GDP. Guanosine Diphosphate eukaryotic translation elongation factor 1 alpha 1 Homo sapiens
11 The results obtained are discussed in terms of the recently described crystal structure of the EF-Tu(mt) x GDP complex. Guanosine Diphosphate eukaryotic translation elongation factor 1 alpha 1 Homo sapiens