Relaxing the Substrate Specificity of an Aminoacyl-tRNA Synthetase Allows in vitro and in vivo Synthesis of Proteins Containing Unnatural Amino Acids

Authors

Michael Ibba, Chapman UniversityFollow
Hauke Hennecke, ETH Zentrum

Document Type

Article

Publication Date

5-15-1995

Abstract

It has previously been demonstrated that the unnatural amino acid p‐Cl‐phenylalanine can be attached to tRNA^Phe by a modified phenylalanyl‐tRNA synthetase with relaxed amino acid substrate specificity. We show that this modification to the translational machinery of Escherichia coli is the only requirement for the incorporation of either p‐Cl‐ or p‐Br‐phenylalanine into full‐length luciferase in vitro. The incorporation of p‐Cl‐phenylalanine was also demonstrated in vivo using a suitably modified host strain. These results represent the first description of the incorporation into a protein in vivo of an unnatural amino acid which is normally rejected by the cellular translational machinery.

Comments

This article was originally published in FEBS Letters, volume 364, in 1995. https://doi.org/10.1016/0014-5793(95)00408-2

Recommended Citation

Ibba, M. and Hennecke, H. (1995) Relaxing the substrate specificity of an aminoacyl-tRNA synthetase allows in vitro and in vivo synthesis of proteins containing unnatural amino acids. FEBS Lett. 364, 272-275. https://doi.org/10.1016/0014-5793(95)00408-2

Copyright

Federation of European Biochemical Societies