ArticleScientific reports2015
Highly reproductive Escherichia coli cells with no specific assignment to the UAG codon.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 107 papers.
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Who cites it
107 citing papers in PubMed, 201 citations in OpenAlex.
- Site-Specific Protein Bioconjugation Through Cellular Incorporation of Noncanonical Amino Acids.Angewandte Chemie (International ed. in English) · 2026Review
- Isosteric Engineering of Enzymes: Overcoming Activity-Stability Trade-Offs by Site-Selective CH → N Substitutions.Angewandte Chemie (International ed. in English) · 2026Article
- An engineered biofactory for efficient production of diverse recombinant superoxide dismutase isozymes loaded with specific metal ions for biochemical characterization.bioRxiv : the preprint server for biology · 2026Article
- Hydrophobic tuning with non-canonical amino acids in a copper metalloenzyme.Nature chemistry · 2026Article
- Cold Orthogonal Translation: A Psychrophilic Pyrrolysyl-tRNA Synthetase Boosts Genetic Code Expansion in E. coli.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Detecting Vibrational Energy Transfer into an Enzyme Active Site via a Transition State Analog.The journal of physical chemistry letters · 2026Article
- Generation of Infectious Prions Amenable to Site-Specific Click Chemistry.ACS chemical biology · 2026Article
- Comparative evaluation of noncanonical amino acids as site-specific NMR probes for the complex of E. coli SSB with single-stranded DNA without isotope labelling.The FEBS journal · 2026Article
- Fluorescent non-canonical amino acid as a site-specific conformational probe of prion formation.bioRxiv : the preprint server for biology · 2026Article
- Entry Without Expression: Internalisation Does Not Predict mRNA Translation for Targeted Lipid Nanoparticles.Small science · 2026Article
- Efficient and Site-Specific Incorporation of 3-Nitro-Tyrosine Into Recombinant Proteins inBio-protocol · 2026Article
- Artificial allosteric protein switches with machine-learning-designed receptors.Nature biotechnology · 2026Article
- Selecting aminoacyl-tRNA synthetase/tRNA pairs for efficient genetic encoding of noncanonical amino acids into proteins.Nature protocols · 2026Review
- Co-Translational Incorporation of (Journal of the American Chemical Society · 2026Article
- Optimization of the genetic code expansion technology for intracellular labelling and single-molecule tracking of proteins in genomically re-codedRSC chemical biology · 2026Article
- Boosting Reversible Photocontrol of a Photoxenase by an Engineered Conformational Shift.Angewandte Chemie (International ed. in English) · 2026Article
- Genetic Encoding of Pentafluorophosphato-Phenylalanine Provides PFAngewandte Chemie (International ed. in English) · 2026Article
- A Robust Bioprocess for the Global Incorporation of Noncanonical Amino Acids in Auxotrophic Hosts Produces Labeled Proteins at the Gram Scale.Chembiochem : a European journal of chemical biology · 2026Article
- Targeted regulatory T cell activation by site-specific PEGylated interleukin-2 mitigates autoimmune inflammation.Journal of translational autoimmunity · 2025Article
- Correlating membrane-protein dynamics with function: Integrating bioinformatics, molecular dynamics, and single-molecule FRET.Protein science : a publication of the Protein Society · 2025Article
47 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Escherichia coli is a widely used host organism for recombinant technology, and the bacterial incorporation of non-natural amino acids promises the efficient synthesis of proteins with novel structures and properties. In the present study, we developed E. coli strains in which the UAG codon was reserved for non-natural amino acids, without compromising the reproductive strength of the host cells. Ninety-five of the 273 UAG stop codons were replaced synonymously in the genome of E. coli BL21(DE3), by exploiting the oligonucleotide-mediated base-mismatch-repair mechanism. This genomic modification allowed the safe elimination of the UAG-recognizing cellular component (RF-1), thus leaving the remaining 178 UAG codons with no specific molecule recognizing them. The resulting strain B-95.ΔA grew as vigorously as BL21(DE3) in rich medium at 25-42°C, and its derivative B-95.ΔAΔfabR was better adapted to low temperatures and minimal media than B-95.ΔA. UAG was reassigned to synthetic amino acids by expressing the specific pairs of UAG-reading tRNA and aminoacyl-tRNA synthetase. Due to the preserved growth vigor, the B-95.ΔA strains showed superior productivities for hirudin molecules sulfonated on a particular tyrosine residue, and the Fab fragments of Herceptin containing multiple azido groups.
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