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Abstract
Faithful translation of the genetic code depends on the GTPase EF-Tu delivering correctly
charged aminoacyl-tRNAs to the ribosome for pairing with cognate codons. The accurate
coupling of cognate amino acids and tRNAs by the aminoacyl-tRNA synthetases is achieved
through a combination of substrate specificity and product editing. Once released
by aminoacyl-tRNA synthetases, both cognate and near-cognate aminoacyl-tRNAs were
considered to be committed to ribosomal protein synthesis through their association
with EF-Tu. Here we show instead that aminoacyl-tRNAs in ternary complex with EF-Tu*GTP
can readily dissociate and rebind to aminoacyl-tRNA synthetases. For mischarged species,
this allows resampling by the product editing pathway, leading to a reduction in the
overall error rate of aminoacyl-tRNA synthesis. Resampling of mischarged tRNAs was
shown to increase the accuracy of translation over ten fold during in vitro protein
synthesis, supporting the presence of an additional quality control step prior to
translation elongation.