Photo-dependent protein biosynthesis using a caged aminoacyl-tRNA

Bioorg Med Chem Lett. 2014 Dec 1;24(23):5369-72. doi: 10.1016/j.bmcl.2014.10.053.

Abstract

Translation systems with four-base codons provide a powerful strategy for protein engineering and protein studies because they enable site-specific incorporation of non-natural amino acids into proteins. In this study, a caged aminoacyl-tRNA with a four-base anticodon was synthesized. The caged aminoacyl-tRNA contains a photocleavable nitroveratryloxycarbonyl (NVOC) group. This study showed that the caged aminoacyl-tRNA was not deacylated, did not bind to EF-Tu, and was activated by light. Photo-dependent translation of an mRNA containing the four-base codon was demonstrated using the caged aminoacyl-tRNA.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acids / metabolism*
  • Protein Biosynthesis
  • Protein Engineering
  • RNA, Transfer, Amino Acyl / metabolism*

Substances

  • Amino Acids
  • RNA, Transfer, Amino Acyl