A rationally designed orthogonal synthetase for genetically encoded fluorescent amino acids. Issue 10 (October 2020)

• Record Type: Journal Article
• Authors: Steinberg, Ximena; Galpin, Jason; Nasir, Gibran; Sepúlveda, Romina V.; Ladron de Guevara, Ernesto; Gonzalez-Nilo, Fernando; Islas, Leon D.; Ahern, Christopher A.; Brauchi, Sebastian E.
• Is Part Of: Heliyon. Volume 6:Issue 10(2020)
• Publication Date: 2020-10
• Subjects: Bioorganic chemistry -- Bioinformatics -- Proteins -- Biochemistry -- Molecular biology -- Unnatural amino acids -- Aminoacyl-tRNA synthetase -- Coumarin -- Fluorescence; Research -- Periodicals; Medical sciences -- Periodicals; Natural history -- Periodicals; Social sciences -- Periodicals; Earth sciences -- Periodicals; Physical sciences -- Periodicals; 507.2
• DOI: 10.1016/j.heliyon.2020.e05140
• Languages: English
• ISSNs: 2405-8440

Abstract

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. Abstract : Bioorganic Chemistry; Bioinformatics; Proteins; Biochemistry; Molecular Biology; Unnatural amino acids, aminoacyl-tRNA synthetase, coumarin, fluorescence.