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

  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},
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… 
A 2-thiouridine derivative in tRNAGlu is a positive determinant for aminoacylation by Escherichia coli glutamyl-tRNA synthetase.
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.
Recognition of the Anticodon Loop of tRNAIle 1 by Isoleucyl-tRNA Synthetase from Escherichia coli
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
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
This review will focus on the current understanding of this RNA:protein interaction between Escherichia coli glutaminyl-tRNA synthetase and tRNAG1n.
Switching recognition of two tRNA synthetases with an amino acid swap in a designed peptide.
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.
The anticodon contains a major element of the identity of arginine transfer RNAs.
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
Aminoacyl-tRNA Synthetases: Occurrence, Structure, and Function
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.


In vitro conversion of a methionine to a glutamine-acceptor tRNA.
The present results provide additional evidence that the specificity of aminoacylation by glutaminyl-tRNA synthetase is sensitive to small changes in the nucleotide sequence of noncognate tRNAs and that uridine in the middle position of the anticodon is involved in the recognition of tRNA substrates by this enzyme.
Rare transfer ribonucleic acid essential for phage growth. Nucleotide sequence comparison of normal and mutant T4 isoleucine-accepting transfer ribonucleic acid.
Unexpectedly, the tRNA Ile synthesized in these revertants still retains two unusual structural features found in the wild-type molecule: the opposition of two Up residues in the amino acid acceptor stem and theOpposition of an Ap and a Gp residue in the anticodon stem.
Base substitutions in the wobble position of the anticodon inhibit aminoacylation of E. coli tRNAfMet by E. coli Met-tRNA synthetase.
Results support a model involving direct interaction between Met-tRNA synthetase and the C in the wobble position during aminoacylation of tRNAfMet, which is indistinguishable from native t RNAfMet with respect to its ability to be aminoacylated by E. coli methionyl-tRNAs.
DNA sequence of a T4 transfer RNA gene cluster.
Changing the identity of a tRNA by introducing a G-U wobble pair near the 3' acceptor end.
To investigate the identity of a tRNA, the nucleotides at three computer-identified positions in tRNAPhe (phenylalanine tRNA) were replaced with the corresponding nucleotide from tRNAAla (alanineTRNA), and the resulting tRNA was that of t RNAAla.
Reactions at the termini of tRNA with T4 RNA ligase.
T4 RNA ligase will catalyze the addition of nucleoside 3', 5'-bisphosphates onto the 3' terminus of tRNA resulting in tRNA molecule one nucleotide longer with a 3' terminal phosphate. Under
Studies on T. utilis tRNATyr variants with enzymatically altered D-loop sequences. I. Deletion of the conserved sequence Gm-G and its effects on aminoacylation and conformation.
Results indicate that nucleotide sequences around Gm18-G19 are not essential sites for the recognition of tR NATyr by T. utilis tyrosyl-tRNA synthetase and that tRNATyr variants with an apparently "relaxed" conformation still have full aminoacylation capacities at around 30 degrees C.