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. 2006 Jan 18;128(2):388-9.
doi: 10.1021/ja055467u.

The incorporation of a photoisomerizable amino acid into proteins in E. coli

Mohua Bose  1 , Dan Groff, Jianming Xie, Eric Brustad, Peter G Schultz
Affiliations

The incorporation of a photoisomerizable amino acid into proteins in E. coli

Mohua Bose et al. J Am Chem Soc. .

Abstract

An orthogonal aminoacyl tRNA synthetase/tRNA pair has been evolved that allows the incorporation of the photoisomerizable amino acid phenylalanine-4'-azobenzene (AzoPhe) into proteins in E. coli in response to the amber nonsense codon. Further, we show that AzoPhe can be used to photoregulate the binding affinity of catabolite activator protein to its promoter. The ability to selectively incorporate AzoPhe into proteins at defined sites should make it possible to regulate a variety of biological processes with light, including enzyme, receptor, and ion channel activity.

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