Codon specificity of UGA suppressor tRNATrp from Escherichia coli.
- 1 December 1977
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 74 (12), 5496-5498
- https://doi.org/10.1073/pnas.74.12.5496
Abstract
A synthetic polyribonucleotide, poly(U5,G), was used to study the codon specificity of wild-type and UGA suppressor tRNATrp from E. coli. Phe (UUU) incorporation directed by this synthetic messenger is reduced somewhat by omission from the incubation mixtures of Val (GUU), Leu (UUG) or Cys (UGU). Omission of Cys stimulates Trp incorporation, and this effect is much more pronounced with the UGA suppressor tRNATrp than with wild-type tRNA. The apparent replacement of Cys by Trp is specific, because the omission of Val or Leu slightly inhibits Trp incorporation. The UGA suppressor tRNATrp can probably translate codons of the form UGN (N is any ribonucleotide). The suppressor tRNATrp translates codons that properly match 2 out of the 3 anticodon nucleotides.This publication has 7 references indexed in Scilit:
- Anticodon conformation and accessibility in wild-type and suppressor tryptophan. tRNA from E.coli.Nucleic Acids Research, 1976
- Allosteric mechanism for codon-dependent tRNA selection on ribosomes.Proceedings of the National Academy of Sciences, 1975
- Ribosomal subunit interaction as studied by light scattering. Evidence of different classes of ribosome preparationsBiochemistry, 1975
- Transcription and Translation of Prereplicative Bacteriophage T4 Genes in VitroJournal of Biological Chemistry, 1973
- Translation of the UGA triplet in vitro by tryptophan transfer RNA'sJournal of Molecular Biology, 1971
- Tryptophan transfer RNA as the UGA suppressorJournal of Molecular Biology, 1971