Interaction of elongation factor Tu with the aminoacyl transfer ribonucleic acid dimer Phe-tRNA-Glu-tRNA.

The effect of EF-Tu.GTP on the codon-anticodon interaction of AA-tRNA was studied by using as a model system the interaction of AA-tRNAs with complementary anticodons, namely, dimerization between yeast or Escherichia coli Phe-tRNAPhe (anticodon GmAA) and E. coli Glu-tRNAGlu (anticodon s2UUC) or nonacylated tRNAGlu in the presence or absence of EF-Tu.GTP. The present data indicate that the ternary complexes Phe-tRNA-EF-Tu.GTP and Glu-tRNA-EF-Tu.GTP can form dimers with a binding constant of (0.9 +/- 0.2) X 10(6) M-1, which is identical in magnitude with that of the dimer of the nonacylated tRNAs tRNAPhe-tRNAGlu and also with that of the complex Phe-tRNA-EF-Tu.GTP with nonacylated tRNAGlu. These results show that the anticodon region is not affected by complexation with EF-Tu.GTP; however, this conclusion does not preclude the possibility of structural changes in the anticodon loop that have no effect in energetic terms. In addition, this model codon-anticodon interaction does not stimulate hydrolysis of the GTP bound in the ternary complex.