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Synthetase polyspecificity as a tool to modulate protein function

Authors
Journal
Bioorganic & Medicinal Chemistry Letters
0960-894X
Publisher
Elsevier
Publication Date
Volume
21
Issue
24
Identifiers
DOI: 10.1016/j.bmcl.2011.09.108
Keywords
  • Unnatural Amino Acids
  • Polyspecificity
  • Green Fluorescence Protein
  • Aminoacyl-Trna Synthetase
  • Fluorescence Modulation
Disciplines
  • Biology

Abstract

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.

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