title: Synthetase polyspecificity as a tool to modulate protein function.
abstract: The site-specific incorporation of unnatural amino acids (UAAs) into proteins in bacteria is made possible by the evolution of aminoacyl-tRNA synthetases that selectively recognize and aminoacylate the amino acid of interest. Recently we have discovered that some of the previously evolved aaRSs display a degree of polyspecificity and are capable of recognizing multiple UAAs. Herein we report the polyspecificity of an aaRS evolved to encode a comarin containing amino acid. This polyspecificity was then exploited to introduce several UAAs into the fluorophore of GFP, altering its photophysical properties.
authors: Department of Chemistry, The Scripps Research Institute, 10550 N. Torrey Pines Rd., La Jolla, CA 92037, USA.
authors: Douglas D
authors: DD
authors: Young
authors: Steffen
authors: S
authors: Jockush
authors: Nicholas J
authors: NJ
authors: Turro
authors: Peter G
authors: PG
authors: Schultz
mesh_terms: D000596:Amino Acids / Q000378:metabolism*; D000604:Amino Acyl-tRNA Synthetases / Q000378:metabolism*; D001419:Bacteria / Q000378:metabolism; D049452:Green Fluorescent Proteins / Q000235:genetics / Q000378:metabolism; D013379:Substrate Specificity
chemical_list: D000596:Amino Acids; D049452:Green Fluorescent Proteins; D000604:Amino Acyl-tRNA Synthetases