title: The pyrrolysine translational machinery as a genetic-code expansion tool.
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.
authors.affiliation: Department of Chemistry, The Ohio State University, 100 W 18th Ave., Columbus, OH 43210, USA.
authors.forename: Tomasz
authors.initials: T
authors.lastname: Fekner
authors.forename: Michael K
authors.initials: MK
authors.lastname: Chan
mesh_terms: D000604:Amino Acyl-tRNA Synthetases; D018388:Codon, Terminator; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D056890:Eukaryota / Q000378:metabolism; D005815:Genetic Code; D008239:Lysine / Q000031:analogs & derivatives* / Q000737:chemistry / Q000235:genetics; D017021:Methanosarcina barkeri / Q000235:genetics / Q000378:metabolism; D015202:Protein Engineering; D011994:Recombinant Proteins / Q000235:genetics*
chemical_list: D018388:Codon, Terminator; D011994:Recombinant Proteins; D000604:Amino Acyl-tRNA Synthetases; C456839:pyrrolysine; D008239:Lysine