ArticleChembiochem : a European journal of chemical biology2014
Gleaning unexpected fruits from hard-won synthetases: probing principles of permissivity in non-canonical amino acid-tRNA synthetases.
Article in Chembiochem : a European journal of chemical biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 47 citations in OpenAlex.
- Genetically Encoding Propiolamide Warhead for the Construction of Phage Displayed Cyclic Peptide Library.Chembiochem : a European journal of chemical biology · 2026Article
- Cold Orthogonal Translation: A Psychrophilic Pyrrolysyl-tRNA Synthetase Boosts Genetic Code Expansion in E. coli.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Selecting aminoacyl-tRNA synthetase/tRNA pairs for efficient genetic encoding of noncanonical amino acids into proteins.Nature protocols · 2026Review
- Optimized Directed Evolution of E. coli leucyl-tRNA Synthetase adds many Noncanonical Amino Acids into the Eukaryotic Genetic Code Including Ornithine and NAngewandte Chemie (International ed. in English) · 2025Article
- Genetic Encoding of Phosphorylated Amino Acids into Proteins.Chemical reviews · 2024Review
- Site-specific dual encoding and labeling of proteins via genetic code expansion.Cell chemical biology · 2023Review
- Enabling Genetic Code Expansion and Peptide Macrocyclization in mRNA Display via a Promiscuous Orthogonal Aminoacyl-tRNA Synthetase.Journal of the American Chemical Society · 2023Article
- Tuning phenylalanine fluorination to assess aromatic contributions to protein function and stability in cells.Nature communications · 2023Article
- Crystal Structure of an Archaeal Tyrosyl-tRNA Synthetase Bound to Photocaged L-Tyrosine and Its Potential Application to Time-Resolved X-ray Crystallography.International journal of molecular sciences · 2022Article
- Creating a Selective Nanobody Against 3-Nitrotyrosine Containing Proteins.Frontiers in chemistry · 2022Article
- Synthesis and characterization of fluorescent amino acid dimethylaminoacridonylalanine.ARKIVOC : free online journal of organic chemistry · 2021Article
- Engineering a Polyspecific Pyrrolysyl-tRNA Synthetase by a High Throughput FACS Screen.Scientific reports · 2019Article
- Improving the Fluorescent Probe Acridonylalanine Through a Combination of Theory and Experiment.Journal of physical organic chemistry · 2018Article
- Chemically-defined lactose-based autoinduction medium for site-specific incorporation of non-canonical amino acids into proteins.RSC advances · 2018Article
- Playing with the Molecules of Life.ACS chemical biology · 2018Review
- Expanding the Scope of Single- and Double-Noncanonical Amino Acid Mutagenesis in Mammalian Cells Using Orthogonal Polyspecific Leucyl-tRNA Synthetases.Biochemistry · 2018Article
- Genetic Code Expansion: A Powerful Tool for Understanding the Physiological Consequences of Oxidative Stress Protein Modifications.Oxidative medicine and cellular longevity · 2018Review
- Expanding and reprogramming the genetic code.Nature · 2017Review
- Doping of Green Fluorescent Protein into Superfluid Helium Droplets: Size and Velocity of Doped Droplets.The journal of physical chemistry. A · 2017Article
- Two-Tier Screening Platform for Directed Evolution of Aminoacyl-tRNA Synthetases with Enhanced Stop Codon Suppression Efficiency.Chembiochem : a European journal of chemical biology · 2017Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The site-specific incorporation of non-canonical amino acids (ncAAs) into proteins is an important tool for understanding biological function. Traditionally, each new ncAA targeted for incorporation requires a resource-consuming process of generating new ncAA aminoacyl tRNA synthetase/tRNACUA pairs. However, the discovery that some tRNA synthetases are "permissive", in that they can incorporate multiple ncAAs, means that it is no longer always necessary to develop a new synthetase for each newly desired ncAA. Developing a better understanding of what factors make ncAA synthetases more permissive would increase the utility of this new approach. Here, we characterized two synthetases selected for the same ncAA that have markedly different "permissivity profiles." Remarkably, the more permissive synthetase incorporated an ncAA for which we had not been able to generate a synthetase through de novo selection methods. Crystal structures revealed that the two synthetases recognize their parent ncAA through a conserved core of interactions, with the more permissive synthetase displaying a greater degree of flexibility in its interaction geometries. We also observed that intraprotein interactions not directly involved in ncAA binding can play a crucial role in synthetase permissivity and suggest that optimization of such interactions might provide an avenue to engineering synthetases with enhanced permissivity.
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Registered trials
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