ArticleNucleic acids research2015
Reassignment of a rare sense codon to a non-canonical amino acid in Escherichia coli.
Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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Who cites it
53 citing papers in PubMed.
- Site-Specific Protein Bioconjugation Through Cellular Incorporation of Noncanonical Amino Acids.Angewandte Chemie (International ed. in English) · 2026Review
- Residue-Specific Incorporation of Noncanonical Amino Acids in Auxotrophic Hosts:Chemical reviews · 2025Review
- Genetic Code Expansion: Recent Developments and Emerging Applications.Chemical reviews · 2025Review
- Pyrrolysine Aminoacyl-tRNA Synthetase as a Tool for Expanding the Genetic Code.International journal of molecular sciences · 2025Review
- Engineering Pyrrolysine Systems for Genetic Code Expansion and Reprogramming.Chemical reviews · 2024Review
- Breaking the Degeneracy of Sense Codons - How Far Can We Go?Israel journal of chemistry · 2024Article
- Evolution of Pyrrolysyl-tRNA Synthetase: From Methanogenesis to Genetic Code Expansion.Chemical reviews · 2024Review
- Engineered mRNA-ribosome fusions for facile biosynthesis of selenoproteins.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- iNClusive: a database collecting useful information on non-canonical amino acids and their incorporation into proteins for easier genetic code expansion implementation.Nucleic acids research · 2024Article
- Codon decoding by orthogonal tRNAs interrogates theFrontiers in genetics · 2024Article
- Selective and Site-Specific Incorporation of Nonstandard Amino Acids Within Proteins for Therapeutic Applications.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Screening for Primordial RNA-Peptide Interactions Using High-Density Peptide Arrays.Life (Basel, Switzerland) · 2023Article
- Editorial: Exploring and expanding the protein universe with non-canonical amino acids.Frontiers in molecular biosciences · 2023Article
- Nanoparticles for vaccine and gene therapy: Overcoming the barriers to nucleic acid delivery.Wiley interdisciplinary reviews. Nanomedicine and nanobiotechnology · 2022Review
- Making Sense of "Nonsense" and More: Challenges and Opportunities in the Genetic Code Expansion, in the World of tRNA Modifications.International journal of molecular sciences · 2022Review
- Impact of queuosine modification of endogenousFrontiers in molecular biosciences · 2022Article
- Genetic Code Engineering by Natural and Unnatural Base Pair Systems for the Site-Specific Incorporation of Non-Standard Amino Acids Into Proteins.Frontiers in molecular biosciences · 2022Review
- Codon-Reduced Protein Synthesis With Manipulating tRNA Components in Cell-Free System.Frontiers in bioengineering and biotechnology · 2022Review
- Directed Evolution Pipeline for the Improvement of Orthogonal Translation Machinery for Genetic Code Expansion at Sense Codons.Frontiers in chemistry · 2022Article
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Authors and funding
12 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The immutability of the genetic code has been challenged with the successful reassignment of the UAG stop codon to non-natural amino acids in Escherichia coli. In the present study, we demonstrated the in vivo reassignment of the AGG sense codon from arginine to L-homoarginine. As the first step, we engineered a novel variant of the archaeal pyrrolysyl-tRNA synthetase (PylRS) able to recognize L-homoarginine and L-N(6)-(1-iminoethyl)lysine (L-NIL). When this PylRS variant or HarRS was expressed in E. coli, together with the AGG-reading tRNA(Pyl) CCU molecule, these arginine analogs were efficiently incorporated into proteins in response to AGG. Next, some or all of the AGG codons in the essential genes were eliminated by their synonymous replacements with other arginine codons, whereas the majority of the AGG codons remained in the genome. The bacterial host's ability to translate AGG into arginine was then restricted in a temperature-dependent manner. The temperature sensitivity caused by this restriction was rescued by the translation of AGG to L-homoarginine or L-NIL. The assignment of AGG to L-homoarginine in the cells was confirmed by mass spectrometric analyses. The results showed the feasibility of breaking the degeneracy of sense codons to enhance the amino-acid diversity in the genetic code.
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