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Relaxing the substrate specificity of an aminoacyl-tRNA synthetase allows in vitro and in vivo synthesis of proteins containing unnatural amino acids.
Journal article

Relaxing the substrate specificity of an aminoacyl-tRNA synthetase allows in vitro and in vivo synthesis of proteins containing unnatural amino acids.

  • Ibba M Mikrobiologisches Institut, Eidgenössische Technische Hochschule, ETH Zentrum, Zürich, Switzerland.
  • Hennecke H
  • 1995-05-15
Published in:
  • FEBS letters. - 1995
Chaperonins
Escherichia coli
Fenclonine
Immunosorbent Techniques
Luciferases
Phenylalanine
Phenylalanine-tRNA Ligase
Protein Biosynthesis
Salmonella typhimurium
Structure-Activity Relationship
Substrate Specificity
English 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.
Language
  • English
Open access status
closed
Identifiers
Persistent URL
https://sonar.ch/global/documents/132730
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