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Fidelity Mechanisms of the Aminoacyl-tRNA Synthetases

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Protein Engineering

Part of the book series: Nucleic Acids and Molecular Biology ((NUCLEIC,volume 22))

The central dogma and its accurate interpretation by a large array of biomolecules remains a fascinating process. Understanding its mechanisms of decoding holds tremendous potential for the future of protein engineering. The family of aminoacyl transfer RNA (tRNA) synthetases (AARSs) is at the forefront of this field. While aminoacylation is the primary role of these enzymes, they possess various additional functions that are important to cell survival. An editing activity, which clears incorrectly attached amino acids, minimizes errors in protein synthesis. If this error correction mechanism is disabled, the incorporation of novel amino acids into proteins offers an exciting approach to expand the genetic code (Döring et al. 2001; Nangle et al. 2006). This chapter focuses on the AARSs that have amino acid editing functions with an emphasis on their continuing dynamic role in the field of protein engineering.

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  1. Department of Biochemistry, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA

    A. P. Mascarenhas, S. An, A. E. Rosen & S. A. Martinis

  2. Departments of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210, USA

    K. Musier-Forsyth

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Mascarenhas, A.P., An, S., Rosen, A.E., Martinis, S.A., Musier-Forsyth, K. (2009). Fidelity Mechanisms of the Aminoacyl-tRNA Synthetases. In: Köhrer, C., RajBhandary, U.L. (eds) Protein Engineering. Nucleic Acids and Molecular Biology, vol 22. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-540-70941-1_6

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