Your browser version may not work well with NCBI's Web applications. More information here...
1: J Am Chem Soc. 2006 Jan 18;128(2):388-9.
Related Articles, Links
Click here to read Click here to read
The incorporation of a photoisomerizable amino acid into proteins in E. coli.

Bose M, Groff D, Xie J, Brustad E, Schultz PG.

Department of Chemistry, The Scripps Research Institute, La Jolla, California 92037, USA.

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.

Publication Types:
PMID: 16402807 [PubMed - indexed for MEDLINE]