The pyrrolysine translational machinery as a genetic-code expansion tool |
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Authors: | Fekner Tomasz Chan Michael K |
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Affiliation: | Department of Chemistry, The Ohio State University, 100 W 18th Ave., Columbus, OH 43210, USA. |
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Abstract: | The discovery of pyrrolysine not only expanded the set of the known proteinogenic amino acids but also revealed unusual features of its encoding mechanism. The engagement of a canonical stop codon and a unique aminoacyl-tRNA synthetase-tRNA pair that can be used to accommodate a broad range of unnatural amino acids while maintaining strict orthogonality in a variety of prokaryotic and eukaryotic expression systems has proven an invaluable combination. Within a few years since its properties were elucidated, the pyrrolysine translational machinery has become a popular choice for the synthesis of recombinant proteins bearing a wide variety of otherwise hard-to-introduce functional groups. It is also central to the development of new synthetic strategies that rely on stop-codon suppression. |
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