Mechanism of tRNA-synthetase recognition: role of terminal A

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 tRNA^Phe comprises a recombination step and a consecutive conformational change. In contrast, the reaction between and the cognate synthetase is characterized by a simple one step mechanism. It is concluded that the terminal A is responsible for the ocurrence 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.