Photo-dependent protein biosynthesis using a caged aminoacyl-tRNA

被引：4

作者：

Akahoshi, Akiya ^{[1
]}

Doi, Yoshio ^{[1
]}

Sisido, Masahiko ^{[1
]}

Watanabe, Kazunori ^{[1
]}

Ohtsuki, Takashi ^{[1
]}

机构：

[1] Okayama Univ, Dept Biotechnol, Okayama 7008530, Japan

来源：

BIOORGANIC & MEDICINAL CHEMISTRY LETTERS | 2014年 / 24卷 / 23期

关键词：

Caged aminoacyl-tRNA; Site-specific incorporation; Non-natural amino acid; Translation; Photocleavable group; ELONGATION-FACTOR TU; GENE-EXPRESSION; INTERFERENCE; ACIDS; STREPTAVIDIN; ANALOGS; BINDING; SYSTEMS;

D O I：

10.1016/j.bmcl.2014.10.053

中图分类号：

R914 [药物化学];

学科分类号：

100701 ;

摘要：

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. (C) 2014 Elsevier Ltd. All rights reserved.

引用

页码：5369 / 5372

页数：4

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