Abstract
Three analogs of yeast alanyl tRNA with anticodon loops of different sizes, tRNA75 (no G35 and 5′-terminal phosphate), tRNA77 (one more C between G35 and C36, no 5′-terminal phosphate), and ptRNA79 (with Cm 1Iψ between G35 and C36), were synthesized. In comparison with the reconstituted natural yeast tRNA, the charging activities of the three analogs were 90% (tRNA75), 94.7% (tRNA77), and 104% (ptRNA79). These results supported the conclusion (Yang De-ping and Wang De-bao (T. P. Wang) (1983) Acta Biochim. Biophys. Sin. 15, 83–90) that the anticodon loop of yeast alanyl tRNA was not involved in the interaction between alanyl-tRNA synthetase from rat liver and yeast alanyl tRNA. In contrast, in the rabbit reticulocyte lysate system, the incorporation of alanine in the charged analogs was 0% (tRNA75 and ptRNA79) and 100% (tRNA77). There were significant differences between the incorporation activities of analogs and those of the reconstituted molecule. The reason for these differences in discussed.
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