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Genetic code expansion

Synthetases pick up the PACE

Nature Chemical Biology volume 13, pages 1205–1206 (2017)Cite this article

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Phage-assisted evolution can rapidly improve the efficiency and substrate specificity of orthogonal aminoacyl-tRNA synthetases. Furthermore, the crystal structure of the pyrrolysyl-tRNA synthetase N-terminal domain reveals the basis for these improvements and provides a structural rationale for orthogonality.

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Figure 1: Phage display accelerates the evolution of orthogonal aaRSs.

Debbie Maizels/Springer Nature

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Authors and Affiliations

  1. the Department of Chemistry, Texas A&M University, College Station, Texas, USA

    Jeffery M Tharp & Wenshe R Liu

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  1. Jeffery M Tharp
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  2. Wenshe R Liu
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Correspondence to Wenshe R Liu.

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The authors declare no competing financial interests.

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Tharp, J., Liu, W. Synthetases pick up the PACE. Nat Chem Biol 13, 1205–1206 (2017). https://doi.org/10.1038/nchembio.2516

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