Ribosome-mediated incorporation of a non-standard amino acid into a peptide through expansion of the genetic code

@article{Bain1992RibosomemediatedIO,
  title={Ribosome-mediated incorporation of a non-standard amino acid into a peptide through expansion of the genetic code},
  author={J. D. Bain and Christopher Y. Switzer and Richard Chamberlin and Steven A. Bennert},
  journal={Nature},
  year={1992},
  volume={356},
  pages={537-539}
}
ONE serious limitation facing protein engineers is the availability of only 20 'proteinogenic' amino acids encoded by natural messenger RNA. The lack of structural diversity among these amino acids restricts the mechanistic and structural issues that can be addressed by site-directed mutagenesis. Here we describe a new technology for incorporating non-standard amino acids into polypeptides by ribosome-based translation. In this technology, the genetic code is expanded through the creation of a… 
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218 Citations
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Methods Citations
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218 Citations

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Genetic Code Engineering by Natural and Unnatural Base Pair Systems for the Site-Specific Incorporation of Non-Standard Amino Acids Into Proteins
TLDR
The current status of methods to incorporate new amino acids into proteins by in vitro and in vivo translation systems are introduced, by focusing on the creation of new codon-anticodon interactions, including unnatural base pair systems for genetic alphabet expansion.
Five-base codons for incorporation of nonnatural amino acids into proteins.
TLDR
A novel strategy for nonnatural mutagenesis as well as a novel insight into the mechanism of frameshift suppression is provided by using five-base codon-anticodon pairs.
Strategies for in vitro and in vivo translation with non-natural amino acids.
  • M. Ibba
  • Biology, Chemistry
    Biotechnology & genetic engineering reviews
  • 1996
TLDR
Recent progress in the understanding of aminoacyl-tRNA synthetase-catalyzed tRNA charging suggests that it may ultimately be possible to extend site-directed mutagenesis to growing cells.
Expanding the genetic code.
TLDR
Using this strategy, the genetic code of Escherichia coli has been expanded to incorporate unnatural amino acids with a fidelity rivaling that of natural amino acids.
Introduction of specialty functions by the position-specific incorporation of nonnatural amino acids into proteins through four-base codon/anticodon pairs
TLDR
The extension of translation systems by the introduction of nonnatural amino acids, four-base codon/anticodon pairs, orthogonal tRNAs, and artificial aminoacyl tRNA synthetases, is a promising approach towards the creation of "synthetic microorganisms" with specialty functions.
Expanding the Genetic Code of Escherichia coli
TLDR
A unique transfer RNA/aminoacyl-tRNA synthetase pair has been generated that expands the number of genetically encoded amino acids in Escherichia coli and should provide a general method for increasing the genetic repertoire of living cells to include a variety of amino acids with novel structural, chemical, and physical properties not found in the common 20 amino acids.
Incorporation of non-natural amino acids into proteins.
An unnatural base pair for incorporating amino acid analogs into proteins
TLDR
This coupled transcription–translation system will permit the efficient synthesis of proteins with a tyrosine analog at the desired position in an Escherichia coli cell-free system.
Reprogramming the genetic code
TLDR
The ability to reprogramme cellular translation and genomes to produce non-canonical biopolymers has wide-ranging applications, including in therapeutics, but has yet to be fully realized.
In vitro non-natural amino acid mutagenesis using a suppressor tRNA generated by the cis-acting hepatitis delta virus ribozyme.
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