A rationally designed orthogonal synthetase for genetically encoded fluorescent amino acids

Ximena Steinberg, Jason Galpin, Gibran Nasir, Romina V. Sepúlveda, Ernesto Ladron de Guevara, Fernando Gonzalez-Nilo, Leon D. Islas, Christopher A. Ahern, Sebastian E. Brauchi

Research output: Contribution to journalArticlepeer-review

2 Citations (Scopus)

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.

Original languageEnglish
Article numbere05140
JournalHeliyon
Volume6
Issue number10
DOIs
Publication statusPublished - Oct 2020

Keywords

  • Aminoacyl-tRNA synthetase
  • Biochemistry
  • Bioinformatics
  • Bioorganic chemistry
  • Coumarin
  • Fluorescence
  • Molecular biology
  • Proteins
  • Unnatural amino acids

ASJC Scopus subject areas

  • General

Fingerprint

Dive into the research topics of 'A rationally designed orthogonal synthetase for genetically encoded fluorescent amino acids'. Together they form a unique fingerprint.

Cite this