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. 1977 Jul;4(7):2253–2262. doi: 10.1093/nar/4.7.2253

Mechanism of tRNA-synthetase recognition: role of terminal A.

G Krauss, D Riesner, G Maass
PMCID: PMC342563  PMID: 909773

Abstract

The function of the terminal A of tRNA Phe (yeast) with respect to complex formation with the cognate aminoacyl-tRNA synthetase has been studied using equilibrium and fast kinetic techniques. Removal of the terminal A influences the equilibrium parameters of the tRNA-synthetase interaction only slightly, the mechanism of complex formation, however, is changed significantly. The binding mechanism of unmodified tRNAPhe comprises a recombination step and a consecutive conformational change. In contrast, the reaction between tRNAPheCC and the cognate synthetase is characterized by a simple one step mechanism. It is concluded that the terminal A is responsible for the occurrence of the conformational change of the tRNA-synthetase complex. The conformational change is interpreted as a proper alignment of the terminal A of the tRNA to the active site of the synthetase.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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