Photo-dependent protein biosynthesis using a caged aminoacyl-tRNA

Akiya Akahoshi, Yoshio Doi, Masahiko Sisido, Kazunori Watanabe, Takashi Ohtsuki

Research output: Contribution to journalArticlepeer-review

3 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)5369-5372
Number of pages4
JournalBioorganic and Medicinal Chemistry Letters
Issue number23
Publication statusPublished - Dec 1 2014


  • Caged aminoacyl-tRNA
  • Non-natural amino acid
  • Photocleavable group
  • Site-specific incorporation
  • Translation

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Pharmaceutical Science
  • Drug Discovery
  • Clinical Biochemistry
  • Organic Chemistry


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