title: Photo-dependent protein biosynthesis using a caged aminoacyl-tRNA.
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.
authors.forename: Akiya
authors.initials: A
authors.lastname: Akahoshi
authors.forename: Yoshio
authors.initials: Y
authors.lastname: Doi
authors.forename: Masahiko
authors.initials: M
authors.lastname: Sisido
authors.forename: Kazunori
authors.initials: K
authors.lastname: Watanabe
authors.forename: Takashi
authors.initials: T
authors.lastname: Ohtsuki
mesh_terms: D000596:Amino Acids / Q000378:metabolism*; D014176:Protein Biosynthesis; D015202:Protein Engineering; D012346:RNA, Transfer, Amino Acyl / Q000378:metabolism*
chemical_list: D000596:Amino Acids; D012346:RNA, Transfer, Amino Acyl