期刊
HELIYON
卷 6, 期 10, 页码 -出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.heliyon.2020.e05140
关键词
Bioorganic chemistry; Bioinformatics; Proteins; Biochemistry; Molecular biology; Unnatural amino acids; Aminoacyl-tRNA synthetase; Coumarin; Fluorescence
资金
- DRI-CONICYT/CONACYT grant [PCCI12023]
- Iniciativa Cientifica Milenio (ANID, Chilean Government)
- National Institutes of Health (U.S. Government)
- FONDECYT [1191868, 1170733]
- DGAPA-PAPIIT-UNAM [IN209515, IN203318]
- National Institutes of Health (NIGMS) [GM106569, GM087519]
- Anillo Cientifico [ACT-1401]
The incorporation of non-canonical amino acids into proteins has emerged as a promising strategy to manipulate and study protein structure-function relationships with superior precision in vitro and in vivo. To date, fluorescent non-canonical amino acids (f-ncAA) have been successfully incorporated in proteins expressed in bacterial systems, Xenopus oocytes, and HEK-293T cells. Here, we describe the rational generation of a novel orthogonal aminoacyl-tRNA synthetase based on the E. coli tyrosine synthetase that is capable of encoding the f-ncAA tyr coumarin in HEK-293T cells.
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