ArticleBiochemistry2016
Improved Incorporation of Noncanonical Amino Acids by an Engineered tRNA(Tyr) Suppressor.
Article in Biochemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 38 citations in OpenAlex.
- Cys-tRNAj as a Second Translation Initiator for Priming Proteins with Cysteine in Bacteria.ACS omega · 2025Article
- Computationally Assisted Noncanonical Amino Acid Incorporation.ACS central science · 2025Article
- Optimization of ACE-tRNAs function in translation for suppression of nonsense mutations.Nucleic acids research · 2024Article
- Evolution of Pyrrolysyl-tRNA Synthetase: From Methanogenesis to Genetic Code Expansion.Chemical reviews · 2024Review
- Genetic Encoding of Phosphorylated Amino Acids into Proteins.Chemical reviews · 2024Review
- Orthogonal Translation for Site-Specific Installation of Post-translational Modifications.Chemical reviews · 2024Review
- Truncation-Free Genetic Code Expansion with Tetrazine Amino Acids for Quantitative Protein Ligations.Bioconjugate chemistry · 2023Article
- Functional analysis of protein post-translational modifications using genetic codon expansion.Protein science : a publication of the Protein Society · 2023Review
- Generating EfficientACS chemical biology · 2022Article
- Directed Evolution Pipeline for the Improvement of Orthogonal Translation Machinery for Genetic Code Expansion at Sense Codons.Frontiers in chemistry · 2022Article
- Impact of queuosine modification of endogenousFrontiers in molecular biosciences · 2022Article
- Therapeutic promise of engineered nonsense suppressor tRNAs.Wiley interdisciplinary reviews. RNA · 2021Review
- Bypassing the requirement for aminoacyl-tRNA by a cyclodipeptide synthase enzyme.RSC chemical biology · 2021Article
- Selection and validation of orthogonal tRNA/synthetase pairs for the encoding of unnatural amino acids across kingdoms.Methods in enzymology · 2021Article
- A rationally designed orthogonal synthetase for genetically encoded fluorescent amino acids.Heliyon · 2020Article
- Overcoming Near-Cognate Suppression in a Release Factor 1-Deficient Host with an Improved Nitro-Tyrosine tRNA Synthetase.Journal of molecular biology · 2020Article
- Dissecting Optical Response and Molecular Structure of Fluorescent Proteins With Non-canonical Chromophores.Frontiers in molecular biosciences · 2020Article
- Combating Antimicrobial Resistance With New-To-Nature Lanthipeptides Created by Genetic Code Expansion.Frontiers in microbiology · 2020Review
- Plasticity and Constraints of tRNA Aminoacylation Define Directed Evolution of Aminoacyl-tRNA Synthetases.International journal of molecular sciences · 2019Review
- Chemically-defined lactose-based autoinduction medium for site-specific incorporation of non-canonical amino acids into proteins.RSC advances · 2018Article
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4 authors at 3 institutions in 1 country.
Funding
Abstract
The Methanocaldcoccus jannaschii tyrosyl-tRNA synthetase (TyrRS):tRNA(Tyr) cognate pair has been used to incorporate a large number of noncanonical amino acids (ncAAs) into recombinant proteins in Escherichia coli. However, the structural elements of the suppressor tRNA(Tyr) used in these experiments have not been examined for optimal performance. Here, we evaluate the steady-state kinetic parameters of wild-type M. jannaschii TyrRS and an evolved 3-nitrotyrosyl-tRNA synthetase (nitroTyrRS) toward several engineered tRNA(Tyr) suppressors, and we correlate aminoacylation properties with the efficiency and fidelity of superfolder green fluorescent protein (sfGFP) synthesis in vivo. Optimal ncAA-sfGFP synthesis correlates with improved aminoacylation kinetics for a tRNA(Tyr) amber suppressor with two substitutions in the anticodon loop (G34C/G37A), while four additional mutations in the D and variable loops, present in the tRNA(Tyr) used in all directed evolution experiments to date, are deleterious to function both in vivo and in vitro. These findings extend to three of four other evolved TyrRS enzymes that incorporate distinct ncAAs. Suppressor tRNAs elicit decreases in amino acid Km values for both TyrRS and nitroTyrRS, suggesting that direct anticodon recognition by TyrRS need not be an impediment to superior performance of this orthogonal system and offering insight into novel approaches for directed evolution. The G34C/G37A tRNA(Tyr) may enhance future incorporation of many ncAAs by engineered TyrRS enzymes.
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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.