Abstract
The effect of the aminoacylation on the structure of tRNA Phe from yeast has been studied by equilibrium dialysis experiments. The association constants of oligomers were determined which were complementary to the dihydrouridine-, the anticodon-, the TψC loop; to the extra-arm and to the 3′-terminus of tRNA Phe-A 73, tRNA Phe-A-C-C-3′ NH 2A and Phe-tRNA Phe-A-C-C-3′-NH 2A in which the phenylalanine is bound by a stable amide bond. The results show that removal of the 3′-terminus or aminoacylation of tRNA Phe from yeast does not cause a gross conformational change of the molecule. However, the aminoacylation renders the 3′-terminus inaccessible to binding complementary oligonucleotides. Based on this finding, it is proposed that the α-amino group of Phe-tRNA Phe-A-C-C-3′ NH 2A folds back to the 5′-terminal phosphate to form a salt bridge.
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