Synthetase polyspecificity as a tool to modulate protein function

BIOORGANIC & MEDICINAL CHEMISTRY LETTERS

卷:21

Article

Young, Douglas D.²  Jockush, Steffen¹  Turro, Nicholas J.¹  Schultz, Peter G.² 

[1] Columbia Univ, Dept Chem, New York, NY 10027 USA

[2] Scripps Res Inst, Dept Chem, La Jolla, CA 92037 USA

关键词: Unnatural amino acids;    Polyspecificity;    Green fluorescence protein;    Aminoacyl-tRNA synthetase;    Fluorescence modulation;   

DOI  :  10.1016/j.bmcl.2011.09.108

来源: Elsevier

【 摘 要 】

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. (C) 2011 Elsevier Ltd. All rights reserved.

【 授权许可】

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