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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Amino Acyl-tRNA Synthetases / genetics
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Amino Acyl-tRNA Synthetases / metabolism
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Codon
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Cyclic AMP / chemistry
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Cyclic AMP / metabolism
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Cyclic AMP Receptor Protein
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DNA, Bacterial / genetics
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DNA, Bacterial / metabolism
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Escherichia coli / genetics
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Escherichia coli / metabolism*
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Escherichia coli Proteins / chemistry
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Escherichia coli Proteins / genetics
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Escherichia coli Proteins / metabolism*
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Isomerism
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Kinetics
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Phenylalanine / analogs & derivatives*
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Phenylalanine / chemistry
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Phenylalanine / metabolism
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Photochemistry
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Receptors, Cell Surface / chemistry
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Receptors, Cell Surface / genetics
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Receptors, Cell Surface / metabolism*
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Spectrophotometry, Ultraviolet
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Transcription Factors / chemistry
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Transcription Factors / genetics
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Transcription Factors / metabolism*
Substances
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Codon
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Cyclic AMP Receptor Protein
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DNA, Bacterial
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Escherichia coli Proteins
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Receptors, Cell Surface
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Transcription Factors
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azophenylalanine
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crp protein, E coli
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Phenylalanine
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Cyclic AMP
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Amino Acyl-tRNA Synthetases