1. A rationally designed orthogonal synthetase for genetically encoded fluorescent amino acids
- Author
-
Ximena Steinberg, Jason Galpin, Gibran Nasir, Romina V. Sepúlveda, Ernesto Ladron de Guevara, Fernando Gonzalez-Nilo, Leon D. Islas, Christopher A. Ahern, and Sebastian E. Brauchi
- Subjects
Bioorganic chemistry ,Bioinformatics ,Proteins ,Biochemistry ,Molecular biology ,Unnatural amino acids ,Science (General) ,Q1-390 ,Social sciences (General) ,H1-99 - Abstract
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.
- Published
- 2020
- Full Text
- View/download PDF