Expanding and Reprogramming the Genetic Code of Cells and Animals

被引：385

作者：

Chin, Jason W. ^{[1
]}

机构：

[1] MRC, Mol Biol Lab, Cambridge CB2 OQH, England

来源：

ANNUAL REVIEW OF BIOCHEMISTRY, VOL 83 | 2014年 / 83卷

基金：

英国医学研究理事会;

关键词：

genetic code expansion; amino acid; synthetic biology; protein labeling; tRNA; aminoacyl-tRNA synthetase; ribosome; protein chemistry; bioorthogonal reaction; posttranslational modification; UNNATURAL AMINO-ACIDS; SITE-SPECIFIC INCORPORATION; RNA SYNTHETASE/TRNA PAIRS; NEMATODE CAENORHABDITIS-ELEGANS; TYROSINE TRANSFER-RNA; DIELS-ALDER REACTIONS; IN-VIVO INCORPORATION; ESCHERICHIA-COLI; MAMMALIAN-CELLS; SACCHAROMYCES-CEREVISIAE;

D O I：

10.1146/annurev-biochem-060713-035737

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

070307 [化学生物学]; 071010 [生物化学与分子生物学];

摘要：

Genetic code expansion and reprogramming enable the site-specific incorporation of diverse designer amino acids into proteins produced in cells and animals. Recent advances are enhancing the efficiency of unnatural amino acid incorporation by creating and evolving orthogonal ribosomes and manipulating the genome. Increasing the number of distinct amino acids that can be site-specifically encoded has been facilitated by the evolution of orthogonal quadruplet decoding ribosomes and the discovery of mutually orthogonal synthetase/tRNA pairs. Rapid progress in moving genetic code expansion from bacteria to eukaryotic cells and animals (C. elegans and D. melanogaster) and the incorporation of useful unnatural amino acids has been aided by the development and application of the pyrrolysyl-transfer RNA (tRNA) synthetase/tRNA pair for unnatural amino acid incorporation. Combining chemoselective reactions with encoded amino acids has facilitated the installation of posttranslational modifications, as well as rapid derivatization with diverse fluorophores for imaging.

引用

页码：379 / 408

页数：30

共 139 条

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A method to site-specifically introduce methyllysine into proteins in E. coli [J].