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Science 16 December 1988:
Vol. 242. no. 4885, pp. 1548 - 1551
DOI: 10.1126/science.3144042
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Articles

Science, Vol 242, Issue 4885, 1548-1551
Copyright © 1988 by American Association for the Advancement of Science

articles

Accuracy of in vivo aminoacylation requires proper balance of tRNA and aminoacyl-tRNA synthetase

R Swanson, P Hoben, M Sumner-Smith, H Uemura, L Watson, and D Soll

Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06511.

The fidelity of protein biosynthesis in any cell rests on the accuracy of aminoacylation of tRNA. The exquisite specificity of this reaction is critically dependent on the correct recognition of tRNA by aminoacyl-tRNA synthetases. It is shown here that the relative concentrations of a tRNA and its cognate aminoacyl-tRNA synthetase are normally well balanced and crucial for maintenance of accurate aminoacylation. When Escherichia coli Gln-tRNA synthetase is overproduced in vivo, it incorrectly acylates the supF amber suppressor tRNA(Tyr) with Gln. This effect is abolished when the intracellular concentration of the cognate tRNA(Gln2) is also elevate. These data indicate that the presence of aminoacyl-tRNA synthetase and the cognate tRNAs in complexed form, which requires the proper balance of the two macromolecules, is critical in maintaining the fidelity of protein biosynthesis. Thus, limits exist on the relative levels of tRNAs and aminoacyl-tRNA synthetases within a cell.


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