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…
391 Citations
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References
SHOWING 1-10 OF 31 REFERENCES
In vitro conversion of a methionine to a glutamine-acceptor tRNA.
- Biology, ChemistryBiochemistry
- 1985
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.
Role of anticodon bases in aminoacylation of Escherichia coli methionine transfer RNAs.
- Biology, ChemistryThe Journal of biological chemistry
- 1977
Rare transfer ribonucleic acid essential for phage growth. Nucleotide sequence comparison of normal and mutant T4 isoleucine-accepting transfer ribonucleic acid.
- BiologyBiochemistry
- 1979
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.
- Biology, ChemistryNucleic acids research
- 1983
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.
The gene for a spinach chloroplast isoleucine tRNA has a methionine anticodon.
- BiologyThe Journal of biological chemistry
- 1982
Nucleotide substitution in the amino acid acceptor stem of lysine transfer RNA causes missense suppression.
- BiologyJournal of molecular biology
- 1984
Changing the identity of a tRNA by introducing a G-U wobble pair near the 3' acceptor end.
- Biology, ChemistryScience
- 1988
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.
- Biology, ChemistryNucleic acids research
- 1978
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.
- Biology, ChemistryJournal of biochemistry
- 1985
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.