Facile System for Genetic Incorporation of Two Different Noncanonical Amino Acids into One Protein in Escherichia coli

• Published in: Angewandte Chemie (International ed.) Vol. 49; no. 18; pp. 3211 - 3214
• Main Authors: Wan, Wei, Huang, Ying, Wang, Zhiyong, Russell, William K, Pai, Pei-Jing, Russell, David H, Liu, Wenshe R
• Format: Journal Article
• Language: English
• Published: Weinheim Wiley-VCH Verlag 19.04.2010; WILEY-VCH Verlag; WILEY‐VCH Verlag
• Subjects: amber suppression; Amino acids; Amino Acids - chemistry; Amino Acids - genetics; Amino Acids - metabolism; Escherichia coli; Escherichia coli - genetics; Escherichia coli - metabolism; Escherichia coli Proteins - chemistry; Escherichia coli Proteins - genetics; Escherichia coli Proteins - metabolism; Genes, Bacterial - genetics; genetic code expansion; Genetics; Green Fluorescent Proteins - chemistry; Green Fluorescent Proteins - genetics; Green Fluorescent Proteins - metabolism; Molecular Structure; Mutations; noncanonical amino acids; Pictures; protein engineering; Proteins; Tyrosine-tRNA Ligase - chemistry; Tyrosine-tRNA Ligase - genetics; Tyrosine-tRNA Ligase - metabolism
• ISSN: 1433-7851; 1521-3773
• DOI: 10.1002/anie.201000465

Two's company: Using a wild‐type or evolved PylRS‐pylTUUA pair to suppress ochre mutation and an evolved MjTyrRS‐Mj${{{\rm {\rm tRNA}}{{{\rm {\rm Tyr}}\hfill \atop {\rm {\rm CUA}}\hfill}}}$ pair to suppress amber mutation, two different noncanonical amino acids (NAAs) have been concomitantly incorporated into one protein in E. coli with high efficiency (see picture, with NAAs 1–4; GFP=green‐fluorescent protein).