Encoding multiple unnatural amino acids via evolution of a quadruplet-decoding ribosome

Heinz Neumann, Kaihang Wang, Lloyd Davis, Maria Garcia-Alai and Jason W. Chin ()
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Heinz Neumann: Medical Research Council Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK
Kaihang Wang: Medical Research Council Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK
Lloyd Davis: Medical Research Council Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK
Maria Garcia-Alai: Medical Research Council Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK
Jason W. Chin: Medical Research Council Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK

Nature, 2010, vol. 464, issue 7287, 441-444

Abstract: Protein-designing ribosomes Although chemists can devise novel amino acids with desirable properties, only a few of these amino acids have been successfully introduced into proteins by the cellular machinery. Even then, it is possible to add only one unnatural amino acid to a protein at a time. In theory the use of quadruplet codons, rather than the triplets used in natural protein synthesis, provides added flexibility in the form of extra blank codons available for assignment to unusual amino acids. Natural ribosomes are very inefficient at decoding quadruplets, and cannot be evolved to do it better as they would then misread the entire proteome. Jason Chin and colleagues get around this problem by creating and synthetically evolving parallel or 'orthogonal' ribosomes that efficiently decode quadruple codons using unnatural tRNA synthase/tRNA pairs. This system has the potential to allow the incorporation of up to 200 novel amino acids in genetically encoded designer proteins.

Date: 2010
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DOI: 10.1038/nature08817

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