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J. Biol. Chem., Vol. 259, Issue 12, 7374-7377, 06, 1984

Studies on the role of eukaryotic nucleotide exchange factor in polypeptide chain initiation

DJ Goss, LJ Parkhurst, HB Mehta, CL Woodley and AJ Wahba

Interactions of eukaryotic 5-dimethylaminonaphthalene-1-sulfonyl- initiation factor 2 (eIF-2) from rabbit reticulocytes and the guanine nucleotide exchange factor ( GEF ), Met-tRNAf, GTP, and GDP were monitored by changes in fluorescence anisotropy and radioactive filtration assays. At 1 mM Mg2+, radioactive filtration assays demonstrate that GEF is necessary for nucleotide exchange. We did not observe a GDP dependence in the association reaction of eIF-2 X GEF for GDP concentrations from 0.01 to 20 microM. This is in disagreement with the model: eIF-2 X GDP + GEF in equilibrium eIF-2 X GEF + GDP. The addition of GTP caused a decrease in fluorescence anisotropy which is interpreted as a dissociation of eIF-2 X GEF . We propose an asymmetrical model of ternary complex (eIF-2 X GTP X Met-tRNAf) formation where 1) GDP does not displace GEF and 2) GTP replaces GEF and presumably GDP. For reticulocyte eIF-2, phosphorylation of the alpha subunit greatly inhibits protein synthesis. This inhibition derives neither from failure of GEF to bind to eIF-2(alpha P) nor from greatly enhanced binding of GEF . The inhibition results from the requirement of very high levels of GTP (100 microM) to dissociate the eIF-2(alpha P) X GEF complex.
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G. D. Pavitt, K. V.A. Ramaiah, S. R. Kimball, and A. G. Hinnebusch
eIF2 independently binds two distinct eIF2B subcomplexes that catalyze and regulate guanine-nucleotide exchange
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S. R. Kimball, N. K. Heinzinger, R. L. Horetsky, and L. S. Jefferson
Identification of Interprotein Interactions between the Subunits of Eukaryotic Initiation Factors eIF2 and eIF2B
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