ArticleBiochimica et biophysica acta. General subjects2017
Increasing the fidelity of noncanonical amino acid incorporation in cell-free protein synthesis.
Article in Biochimica et biophysica acta. General subjects, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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15 citing papers in PubMed, 28 citations in OpenAlex.
- Genetic Encoding of Phosphorylated Amino Acids into Proteins.Chemical reviews · 2024Review
- Orthogonal Translation for Site-Specific Installation of Post-translational Modifications.Chemical reviews · 2024Review
- Recoding UAG to selenocysteine inRNA (New York, N.Y.) · 2023Article
- System-wide optimization of an orthogonal translation system with enhanced biological tolerance.Molecular systems biology · 2023Article
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- Genetic Code Expansion in the Engineered Organism Vmax X2: High Yield and Exceptional Fidelity.ACS central science · 2021Article
- New developments in RiPP discovery, enzymology and engineering.Natural product reports · 2021Review
- Overcoming Near-Cognate Suppression in a Release Factor 1-Deficient Host with an Improved Nitro-Tyrosine tRNA Synthetase.Journal of molecular biology · 2020Article
- Chimeric Translation for Mitochondrial Peptides: Regular and Expanded Codons.Computational and structural biotechnology journal · 2019Article
- Advances and Challenges in Cell-Free Incorporation of Unnatural Amino Acids Into Proteins.Frontiers in pharmacology · 2019Review
- The Application of Cell-Free Protein Synthesis in Genetic Code Expansion for Post-translational Modifications.Frontiers in pharmacology · 2019Review
- In vitro genetic code reprogramming and expansion to study protein function and discover macrocyclic peptide ligands.Current opinion in chemical biology · 2018Review
- Genetically encoded amino acids with tert-butyl and trimethylsilyl groups for site-selective studies of proteins by NMR spectroscopy.Journal of biomolecular NMR · 2018Article
- Characterizing Lysine Acetylation of Isocitrate Dehydrogenase in Escherichia coli.Journal of molecular biology · 2018Article
- Genetically Incorporating Two Distinct Post-translational Modifications into One Protein Simultaneously.ACS synthetic biology · 2018Article
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2 authors at 1 institution in 1 country.
Funding
Abstract
backgroundCell-free protein synthesis provides a robust platform for co-translational incorporation of noncanonical amino acid (ncAA) into proteins to facilitate biological studies and biotechnological applications. Recently, eliminating the activity of release factor 1 has been shown to increase ncAA incorporation in response to amber codons. However, this approach could promote mis-incorporation of canonical amino acids by near cognate suppression.
methodsWe performed a facile protocol to remove near cognate tRNA isoacceptors of the amber codon from total tRNAs, and used the phosphoserine (Sep) incorporation system as validation. By manipulating codon usage of target genes and tRNA species introduced into the cell-free protein synthesis system, we increased the fidelity of Sep incorporation at a specific position.
resultsBy removing three near cognate tRNA isoacceptors of the amber stop codon [tRNA
conclusionsRemoval of near cognate tRNA isoacceptors of the amber codon could increase ncAA incorporation fidelity towards the amber stop codon in release factor deficiency systems. GENERAL SIGNIFICANCE: We provide a general strategy to improve fidelity of ncAA incorporation towards stop, quadruplet and sense codons in cell-free protein synthesis systems. This article is part of a Special Issue entitled "Biochemistry of Synthetic Biology - Recent Developments" Guest Editor: Dr. Ilka Heinemann and Dr. Patrick O'Donoghue.
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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.