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The fidelity of translation is determined at two major points: the accuracy of aminoacyl-tRNA selection by the ribosomes and synthesis of cognate amino acid/tRNA pairs by aminoacyl-tRNA synthetases (aaRSs) in the course of the aminoacylation reaction. The most important point in aminoacylation is the accurate recognition of cognate substrates coupled with discrimination of non-cognates. While this is generally accomplished by a single enzyme, we have recently found that discrimination against lysine analogues requires the existence of two unrelated lysyl-tRNA synthetases. For other amino acids, initial recognition is not sufficiently accurate with errors being corrected by an intrinsic editing activity. Recent studies indicate how editing prevents the misinterpretation of phenylalanine as tyrosine in the genetic code and have shown the importance of this process in vivo . More recent studies indicate that while these editing reactions are critical in the cytoplasm, some are absent from mitochondria suggesting that the overall idelity of protein synthesis might be reduced in this compartment.


This article was originally published in Chemistry in Industry, volume 55, in 2006.


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