ArticleNucleic acids research2018
Oligonucleotide-mediated tRNA sequestration enables one-pot sense codon reassignment in vitro.
Article in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers, 1 of them a synthesis that pooled it.
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Who cites it
23 citing papers in PubMed, 1 synthesis or guideline pooled it, 46 citations in OpenAlex.
- Cell-Free Approach for Non-canonical Amino Acids Incorporation Into Polypeptides.Frontiers in bioengineering and biotechnology · 2020Pooled it
- DNA oligonucleotides encoding suppressor tRNA induce readthrough of premature termination codon.Molecular therapy. Nucleic acids · 2026Article
- Developing antisense oligomer biotics "asobiotics" as precision antibacterials: designs, strategies, and considerations for future success.FEMS microbiology reviews · 2026Review
- Chemical and ribosomal synthesis of atropisomeric and macrocyclic peptides with embedded quinolines.Nature chemistry · 2026Article
- BeyondChemical reviews · 2025Review
- Cell-Free Gene Expression: Methods and Applications.Chemical reviews · 2025Review
- Breaking the Degeneracy of Sense Codons - How Far Can We Go?Israel journal of chemistry · 2024Article
- Engineering tRNAs for the Ribosomal Translation of Non-proteinogenic Monomers.Chemical reviews · 2024Review
- Selective thiazoline peptide cyclisation compatible with mRNA display and efficient synthesis.Chemical science · 2023Article
- Extensive breaking of genetic code degeneracy with non-canonical amino acids.Nature communications · 2023Article
- Cell-Free Display Techniques for Protein Evolution.Advances in biochemical engineering/biotechnology · 2023Article
- Opportunities for Expanding Encoded Chemical Diversification and Improving Hit Enrichment in mRNA-Displayed Peptide Libraries.Chembiochem : a European journal of chemical biology · 2022Review
- Towards a generic prototyping approach for therapeutically-relevant peptides and proteins in a cell-free translation system.Nature communications · 2022Article
- Codon-Reduced Protein Synthesis With Manipulating tRNA Components in Cell-Free System.Frontiers in bioengineering and biotechnology · 2022Review
- Cell-Free PURE System: Evolution and Achievements.Biodesign research · 2022Review
- Rational Design of Aptamer-Tagged tRNAs.International journal of molecular sciences · 2020Article
- Cell-free gene expression: an expanded repertoire of applications.Nature reviews. Genetics · 2020Review
- Strategies for in vitro engineering of the translation machinery.Nucleic acids research · 2020Review
- Review
- Emerging Methods for Efficient and Extensive Incorporation of Non-canonical Amino Acids Using Cell-Free Systems.Frontiers in bioengineering and biotechnology · 2020Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Sense codon reassignment to unnatural amino acids (uAAs) represents a powerful approach for introducing novel properties into polypeptides. The main obstacle to this approach is competition between the native isoacceptor tRNA(s) and orthogonal tRNA(s) for the reassigned codon. While several chromatographic and enzymatic procedures for selective deactivation of tRNA isoacceptors in cell-free translation systems exist, they are complex and not scalable. We designed a set of tRNA antisense oligonucleotides composed of either deoxy-, ribo- or 2'-O-methyl ribonucleotides and tested their ability to efficiently complex tRNAs of choice. Methylated oligonucleotides targeting sequence between the anticodon and variable loop of tRNASerGCU displayed subnanomolar binding affinity with slow dissociation kinetics. Such oligonucleotides efficiently and selectively sequestered native tRNASerGCU directly in translation-competent Escherichia coli S30 lysate, thereby, abrogating its translational activity and liberating the AGU/AGC codons. Expression of eGFP protein from the template harboring a single reassignable AGU codon in tRNASerGCU-depleted E. coli lysate allowed its homogeneous modification with n-propargyl-l-lysine or p-azido-l-phenylalanine. The strategy developed here is generic, as demonstrated by sequestration of tRNAArgCCU isoacceptor in E. coli translation system. Furthermore, this method is likely to be species-independent and was successfully applied to the eukaryotic Leishmania tarentolae in vitro translation system. This approach represents a new direction in genetic code reassignment with numerous practical applications.
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