Chimeric design of pyrrolysyl-tRNA synthetase/tRNA pairs and canonical synthetase/tRNA pairs for genetic code expansion

• Published in: Nature communications Vol. 11; no. 1; pp. 3154 - 13
• Main Authors: Ding, Wenlong, Zhao, Hongxia, Chen, Yulin, Zhang, Bin, Yang, Yang, Zang, Jia, Wu, Jing, Lin, Shixian
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 22.06.2020; Nature Publishing Group; Nature Portfolio
• Subjects: 14/35; 631/61/338/552; 631/92/469; 639/638/92/2783; 82/58; 82/80; 82/83; Alanine; Alanine - analogs & derivatives; Amino acids; Amino Acids - biosynthesis; Aminoacyl-tRNA ligase; Chimera - genetics; Chimera - metabolism; Chimeras; Design; E coli; Escherichia coli; Eukaryotes; Fluorescence; Genetic Code; HEK293 Cells; Histidine; Histidine - analogs & derivatives; Humanities and Social Sciences; Humans; Lysine - analogs & derivatives; Mammalian cells; Mammals; multidisciplinary; Orthogonality; Phenylalanine; Phenylalanine - analogs & derivatives; Post-translation; Prokaryotes; RNA, Transfer - genetics; RNA, Transfer - metabolism; Science; Science (multidisciplinary); Synthetic Biology - methods; Translation; tRNA Ala; tRNA His; Tryptophan; Tryptophan - analogs & derivatives; Tyrosine; Tyrosine - analogs & derivatives

An orthogonal aminoacyl-tRNA synthetase/tRNA pair is a crucial prerequisite for site-specific incorporation of unnatural amino acids. Due to its high codon suppression efficiency and full orthogonality, the pyrrolysyl-tRNA synthetase/pyrrolysyl-tRNA pair is currently the ideal system for genetic cod...