ABSTRACT
The recognition of a transfer ribonucleic acid (tRNA) by its aminoacyl-tRNA synthetase is a classic example of the specificity often encountered in biology. Central to the study of tRNA aminoacylation is the identification of the set of nucleotides in a given tRNA allowing efficient aminoacylation exclusively by the cognate synthetase. The anticodon is also one of the only domains where no two tRNAs will have the same sequence, and so, could act as a site of discrimination by aminoacyl-tRNA synthetases. There have typically been both in vitro and in vivo approaches to the study of tRNA identity. The ideal in vivo system would be one in which mutations could be introduced into a test tRNA without having to alter its natural anticodon. The overwhelming majority of results point to nucleotides of the anticodon, in addition to nucleotides in the distal part of the acceptor arm, as playing the largest role in recognition by aminoacyl-tRNA synthetases.
