期刊
ANNUAL REVIEW OF BIOCHEMISTRY, VOL 83
卷 83, 期 -, 页码 379-408出版社
ANNUAL REVIEWS
DOI: 10.1146/annurev-biochem-060713-035737
关键词
genetic code expansion; amino acid; synthetic biology; protein labeling; tRNA; aminoacyl-tRNA synthetase; ribosome; protein chemistry; bioorthogonal reaction; posttranslational modification
资金
- MRC [MC_U105181009] Funding Source: UKRI
- Medical Research Council [MC_U105181009] Funding Source: researchfish
- Medical Research Council [MC_U105181009] Funding Source: Medline
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.
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