A Designed Phenylalanyl-tRNA Synthetase Variant Allows Efficient in Vivo Incorporation of Aryl Ketone Functionality into Proteins

Incorporation of non-natural amino acids into proteins in vivo expands the scope of protein synthesis and design. p-Acetylphenylalanine was incorporated into recombinant dihydrofolate reductase (DHFR) in Escherichia coli via a computationally designed mutant form of the phenylalanyl-tRNA synthetase...

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Bibliographic Details
Published in:Journal of the American Chemical Society 2002-05, Vol.124 (20), p.5652-5653
Main Authors: Datta, Deepshikha, Wang, Pin, Carrico, Isaac S, Mayo, Stephen L, Tirrell, David A
Format: Article
Language:English
Subjects:
Analytical, structural and metabolic biochemistry
Biological and medical sciences
Enzymes and enzyme inhibitors
Escherichia coli - enzymology
Escherichia coli - genetics
Fundamental and applied biological sciences. Psychology
Ketones - metabolism
Ligases
Mutagenesis
Phenylalanine - analogs & derivatives
Phenylalanine - metabolism
Phenylalanine-tRNA Ligase - genetics
Phenylalanine-tRNA Ligase - metabolism
Recombinant Proteins - genetics
Recombinant Proteins - metabolism
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Summary:Incorporation of non-natural amino acids into proteins in vivo expands the scope of protein synthesis and design. p-Acetylphenylalanine was incorporated into recombinant dihydrofolate reductase (DHFR) in Escherichia coli via a computationally designed mutant form of the phenylalanyl-tRNA synthetase of the host. DHFR outfitted with ketone functionality can be chemoselectively ligated with hydrazide reagents under mild conditions.
ISSN:0002-7863
1520-5126
DOI:10.1021/ja0177096