Abstract
This paper presents data on the structure and function of tRNA and aminoacyl synthetases at high temperatures. The aminoacylating system from Thermus aquaticus was found to be more thermostable and biologically active at much higher temperatures than the aminoacylating sytem from Escherichia coli. The optimum temperature for the formation of phenylalanyl- and isoleucyl-tRNA from T. aquaticus was 70°, whereas the optimum temperature in E. coli was 45°. Both the tRNA and the aminoacylating enzymes of T. aquaticus were more thermostable than those of E. coli. The temperature optima in heterologous systems reflected the heat sensitivity of the E. coli component. Both reversible and irreversible effects of heat on the E. coli tRNA could be detected. These data provide further evidence that thermophily is achieved by virtue of inherently thermal stable constituents which have high temperature optima for biological function.
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