Glutamyl‐tRNA synthetase (GluRS) from barley chloroplasts is a naturally occurring mischarging enzyme: it efficiently aminoacylates both the homologous tRNAGlu as well as tRNAGln species. In order to shed light on the structural requirements of this enzyme for tRNA specificity heterologous charging experiments were performed. Sequence comparison of tRNAs recognized by barley chloroplast GluRS reveals that two base pairs, one in the acceptor stem and one in the anticodon stem, appear to be critical for substrate recognition.
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Schön et al. (1988) studied this question.
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