ArticleProceedings of the National Academy of Sciences of the United States of America1997
Engineering a tRNA and aminoacyl-tRNA synthetase for the site-specific incorporation of unnatural amino acids into proteins in vivo.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.
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Who cites it
58 citing papers in PubMed, 183 citations in OpenAlex.
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- Engineering Phages to Fight Multidrug-Resistant Bacteria.Chemical reviews · 2025Review
- Genetic Code Expansion for Mechanistic Studies in Ion Channels: An (Un)natural Union of Chemistry and Biology.Chemical reviews · 2024Review
- Cracking the Code: Reprogramming the Genetic Script in Prokaryotes and Eukaryotes to Harness the Power of Noncanonical Amino Acids.Chemical reviews · 2024Review
- Engineered Proteins and Materials Utilizing Residue-Specific Noncanonical Amino Acid Incorporation.Chemical reviews · 2024Review
- Applications of genetic code expansion technology in eukaryotes.Protein & cell · 2024Review
- tRNA engineering strategies for genetic code expansion.Frontiers in genetics · 2024Review
- Engineering synthetic biomolecular condensates.Nature reviews bioengineering · 2023Review
- Advancing synthetic biology through cell-free protein synthesis.Computational and structural biotechnology journal · 2023Review
- Expanding the chemical diversity of M13 bacteriophage.Frontiers in microbiology · 2022Review
- Genetic Code Expansion in the Engineered Organism Vmax X2: High Yield and Exceptional Fidelity.ACS central science · 2021Article
- A self-labeling protein based on the small ultra-red fluorescent protein, smURFP.RSC chemical biology · 2021Article
- Reprogramming the genetic code.Nature reviews. Genetics · 2021Review
- Post-Translational Modifications of CytochromeInternational journal of molecular sciences · 2020Review
- Plasticity and Constraints of tRNA Aminoacylation Define Directed Evolution of Aminoacyl-tRNA Synthetases.International journal of molecular sciences · 2019Review
- Substituting the catalytic proline of 4-oxalocrotonate tautomerase with non-canonical analogues reveals a finely tuned catalytic system.Scientific reports · 2019Article
- Translational Control using an Expanded Genetic Code.International journal of molecular sciences · 2019Review
- Playing with the Molecules of Life.ACS chemical biology · 2018Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In an effort to expand the scope of protein mutagenesis, we have completed the first steps toward a general method to allow the site-specific incorporation of unnatural amino acids into proteins in vivo. Our approach involves the generation of an "orthogonal" suppressor tRNA that is uniquely acylated in Escherichia coli by an engineered aminoacyl-tRNA synthetase with the desired unnatural amino acid. To this end, eight mutations were introduced into tRNA2Gln based on an analysis of the x-ray crystal structure of the glutaminyl-tRNA aminoacyl synthetase (GlnRS)-tRNA2Gln complex and on previous biochemical data. The resulting tRNA satisfies the minimal requirements for the delivery of an unnatural amino acid: it is not acylated by any endogenous E. coli aminoacyl-tRNA synthetase including GlnRS, and it functions efficiently in protein translation. Repeated rounds of DNA shuffling and oligonucleotide-directed mutagenesis followed by genetic selection resulted in mutant GlnRS enzymes that efficiently acylate the engineered tRNA with glutamine in vitro. The mutant GlnRS and engineered tRNA also constitute a functional synthetase-tRNA pair in vivo. The nature of the GlnRS mutations, which occur both at the protein-tRNA interface and at sites further away, is discussed.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.