ArticleNucleic acids research2003
An archaebacteria-derived glutamyl-tRNA synthetase and tRNA pair for unnatural amino acid mutagenesis of proteins in Escherichia coli.
Article in Nucleic acids research, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 75 citations in OpenAlex.
- Genetic Code Expansion: Recent Developments and Emerging Applications.Chemical reviews · 2025Review
- Cellular Site-Specific Incorporation of Noncanonical Amino Acids in Synthetic 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
- Enhanced Directed Evolution in Mammalian Cells Yields a Hyperefficient Pyrrolysyl tRNA for Noncanonical Amino Acid Mutagenesis.Angewandte Chemie (International ed. in English) · 2024Article
- Tuning tRNAs for improved translation.Frontiers in genetics · 2024Review
- Ferritin nanocages as efficient nanocarriers and promising platforms for COVID-19 and other vaccines development.Biochimica et biophysica acta. General subjects · 2023Review
- Ferritin-based nanomedicine for disease treatment.Medical review (2021) · 2023Review
- "Not-so-popular" orthogonal pairs in genetic code expansion.Protein science : a publication of the Protein Society · 2023Review
- A Simplified Protocol to Incorporate the Fluorescent Unnatural Amino Acid ANAP into Xenopus laevis Oocyte-Expressed P2X7 Receptors.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Reprogramming the genetic code.Nature reviews. Genetics · 2021Review
- Rapid discovery and evolution of orthogonal aminoacyl-tRNA synthetase-tRNA pairs.Nature biotechnology · 2020Article
- Site-Specific Incorporation of Unnatural Amino Acids into Escherichia coli Recombinant Protein: Methodology Development and Recent Achievement.Biomolecules · 2019Review
- Plasticity and Constraints of tRNA Aminoacylation Define Directed Evolution of Aminoacyl-tRNA Synthetases.International journal of molecular sciences · 2019Review
- Playing with the Molecules of Life.ACS chemical biology · 2018Review
- Ferritin Nanocages with Biologically Orthogonal Conjugation for Vascular Targeting and Imaging.Bioconjugate chemistry · 2018Article
- Expanding and reprogramming the genetic code.Nature · 2017Review
- Future of the Genetic Code.Life (Basel, Switzerland) · 2017Review
- At the Interface of Chemical and Biological Synthesis: An Expanded Genetic Code.Cold Spring Harbor perspectives in biology · 2016Review
- Coevolution Theory of the Genetic Code at Age Forty: Pathway to Translation and Synthetic Life.Life (Basel, Switzerland) · 2016Article
- Overcoming Challenges in Engineering the Genetic Code.Journal of molecular biology · 2016Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The addition of novel amino acids to the genetic code of Escherichia coli involves the generation of an aminoacyl-tRNA synthetase and tRNA pair that is 'orthogonal', meaning that it functions independently of the synthetases and tRNAs endogenous to E.coli. The amino acid specificity of the orthogonal synthetase is then modified to charge the corresponding orthogonal tRNA with an unnatural amino acid that is subsequently incorporated into a polypeptide in response to a nonsense or missense codon. Here we report the development of an orthogonal glutamic acid synthetase and tRNA pair. The tRNA is derived from the consensus sequence obtained from a multiple sequence alignment of archaeal tRNA(Glu) sequences. The glutamyl-tRNA synthetase is from the achaebacterium Pyrococcus horikoshii. The new orthogonal pair suppresses amber nonsense codons with an efficiency roughly comparable to that of the orthogonal tyrosine pair derived from Methanococcus jannaschii, which has been used to selectively incorporate a variety of unnatural amino acids into proteins in E.coli. Development of the glutamic acid orthogonal pair increases the potential diversity of unnatural amino acid structures that may be incorporated into proteins in E.coli.
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Registered trials
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.