ArticleNature chemistry2021
A 68-codon genetic code to incorporate four distinct non-canonical amino acids enabled by automated orthogonal mRNA design.
Article in Nature chemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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Who cites it
50 citing papers in PubMed.
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- Genetic Incorporation of Diverse Noncanonical Amino Acids for Histidine Substitution.Journal of the American Chemical Society · 2026Article
- Continuous evolution of a halogenase enzyme with improved solubility and activity for sustainable bioproduction.Nature communications · 2026Article
- A reprogrammed genetic code consisting of 32 distinct amino acids.Nucleic acids research · 2026Article
- Protein-Membrane Interactions Studied by Transmission and Total Internal Reflection FTIR Spectroscopy.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Efficient genetic code expansion without host genome modifications.Nature biotechnology · 2025Article
- Recoded gene circuits for multiplexed genetic code expansion.Nature biotechnology · 2025Article
- The design and engineering of synthetic genomes.Nature reviews. Genetics · 2025Review
- Fluorescent labeling strategies for molecular bioimaging.Biophysical reports · 2025Review
- Expanding the genetic code: In vivo approaches for incorporating non-proteinogenic monomers.Journal of microbiology (Seoul, Korea) · 2025Review
- BeyondChemical reviews · 2025Review
- Automated Flow Synthesis of Artificial Heme Enzymes for Enantiodivergent Biocatalysis.Journal of the American Chemical Society · 2025Article
- 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
- Quadruplet codon decoding-based versatile genetic biocontainment system.Nucleic acids research · 2025Article
- Article
- Recent advances in the expanding genetic code.Current opinion in chemical biology · 2024Review
- Noncanonical Amino Acid Tools and Their Application to Membrane Protein Studies.Chemical reviews · 2024Review
- Assembly of functional microbial ecosystems: from molecular circuits to communities.FEMS microbiology reviews · 2024Review
- Directed Evolution ofACS bio & med chem Au · 2024Article
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4 authors.
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Abstract
Orthogonal (O) ribosome-mediated translation of O-mRNAs enables the incorporation of up to three distinct non-canonical amino acids (ncAAs) into proteins in Escherichia coli (E. coli). However, the general and efficient incorporation of multiple distinct ncAAs by O-ribosomes requires scalable strategies for both creating efficiently and specifically translated O-mRNAs, and the compact expression of multiple O-aminoacyl-tRNA synthetase (O-aaRS)/O-tRNA pairs. We automate the discovery of O-mRNAs that lead to up to 40 times more protein, and are up to 50-fold more orthogonal, than previous O-mRNAs; protein yields from our O-mRNAs match or exceed those from wild-type mRNAs. These advances enable a 33-fold increase in yield for incorporating three distinct ncAAs. We automate the creation of operons for O-tRNA genes, and develop operons for O-aaRS genes. Combining our advances creates a 68-codon, 24-amino-acid genetic code to efficiently incorporate four distinct ncAAs into a single protein in response to four distinct quadruplet codons.
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