Codon and amino-acid specificities of a transfer RNA are both converted by a single post-transcriptional modification

@article{Muramatsu1988CodonAA,
  title={Codon and amino-acid specificities of a transfer RNA are both converted by a single post-transcriptional modification},
  author={Tomonari Muramatsu and Kazuya Nishikawa and Fumiko Nemoto and Yoshiyuki Kuchino and Susumu Nishimura and Tatsuo Miyazawa and Shigeyuki Yokoyama},
  journal={Nature},
  year={1988},
  volume={336},
  pages={179-181}
}
An Escherichia coli isoleucine transfer RNA specific for the codon AUA (tRNA2Ile or tRNAminorIle (ref. 1) has a novel modified nucleo-side, lysidine (L; ref. 2) (Fig. la) in the first position of the anticodon (position 34), which is essential for the specific recognition of the codon AUA (ref. 1). We isolated the gene for tRNA2Ile (ileX) and found that the anticodon is CAT, which is characteristic of the methionine tRNA gene. Replacement of L(34) of tRNA2Ile molecule enzymatically with… 
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391 Citations

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TLDR
It is shown conclusively that the modified uridine at position 34 in tRNA(Glu) is required for efficient aminoacylation by E. coli GluRS, only the second example of a tRNA modification acting as a positive determinant for interaction with its cognate aminoacyl-tRNA synthetase.
Enzymatic conversion of cytidine to lysidine in anticodon of bacterial tRNAIle – an alternative way of RNA editing
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A variant with replacement of the N-((9-β-D-ribofuranosyl-purine-6-yl)carbamoyl)threonine (t6A) residue at position 37 with an unmodified adeno-sine exhibited a drastic reduction in isoleucine-accepting activity, showing that t6A37 plays a crucial role in the recognition by isoleucyl-tRNA synthetase (IleRS).
Structural basis for translational fidelity ensured by transfer RNA lysidine synthetase
TLDR
It is shown that the TilS enzyme specifically recognizes and modifies tRNAIle2 in its precursor form, thereby avoiding translation errors and providing a rationale for the necessity of incorporating specific modifications at the precursor level during tRNA biogenesis.
Specificity in RNA: Protein Interactions; the Recognition of Escherichia Coli Glutamine tRNA
TLDR
This review will focus on the current understanding of this RNA:protein interaction between Escherichia coli glutaminyl-tRNA synthetase and tRNAG1n.
molecular mechanism of lysidine synthesis that determines tRNA identity and codon recognition.
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TLDR
Results of combinatorial mutagenesis of an anticodon-binding-helix loop peptide were used to design a hybrid sequence composed of amino acid residues from methionyl- and isoleucyl-tRNA synthetases, and the swap of a single amino acid in the transplanted peptide switches specificity between anticodons that differ by one nucleotide.
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The contribution of the anticodon to the discrimination between cognate and noncognate tRNAs by Escherichia coli Arg-tRNA synthetase has been investigated by in vitro synthesis and aminoacylation of…
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The present knowledge indicates that each of these functions is distributed along the aaRS polypeptide through the formation of specialized domains, including activation of the amino acid and recognition of the tRNA molecule.
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