在大肠杆菌中将一种光可异构化氨基酸掺入蛋白质中。

The incorporation of a photoisomerizable amino acid into proteins in E. coli.

作者信息

Bose Mohua, Groff Dan, Xie Jianming, Brustad Eric, Schultz Peter G

机构信息

Department of Chemistry, The Scripps Research Institute, La Jolla, California 92037, USA.

出版信息

J Am Chem Soc. 2006 Jan 18;128(2):388-9. doi: 10.1021/ja055467u.

DOI:10.1021/ja055467u

PMID:16402807

Abstract

An orthogonal aminoacyl tRNA synthetase/tRNA pair has been evolved that allows the incorporation of the photoisomerizable amino acid phenylalanine-4'-azobenzene (AzoPhe) into proteins in E. coli in response to the amber nonsense codon. Further, we show that AzoPhe can be used to photoregulate the binding affinity of catabolite activator protein to its promoter. The ability to selectively incorporate AzoPhe into proteins at defined sites should make it possible to regulate a variety of biological processes with light, including enzyme, receptor, and ion channel activity.

摘要

一种正交氨酰-tRNA合成酶/tRNA对已经进化出来，它能够使可光异构化的氨基酸苯丙氨酸-4'-偶氮苯（AzoPhe）在大肠杆菌中响应琥珀色无义密码子而掺入蛋白质中。此外，我们表明AzoPhe可用于光调节分解代谢物激活蛋白与其启动子的结合亲和力。在特定位点选择性地将AzoPhe掺入蛋白质的能力应该使得用光调节各种生物过程成为可能，包括酶、受体和离子通道的活性。