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Flavin-Tag
- Source :
- BIOCONJUGATE CHEMISTRY, 32(8), 1559-1563. AMER CHEMICAL SOC
- Publication Year :
- 2021
-
Abstract
- Site-specific protein labeling methods are highly valuable tools for research and applications. We present a new protein labeling method that allows covalent attachment of a chromo-and fluorogenic flavin (FMN) to any targeted protein using a short flavinylation peptide-Tag. We show that this peptide can be as short as 7 residues and can be located at the N-Terminus, C-Terminus, or in internal regions of the target protein. Analogous to kinase-catalyzed phosphorylation, the flavin is covalently attached via a stable phosphothreonyl linkage. The site-specific covalent tethering of FMN is accomplished by using a bacterial flavin transferase. The covalent coupling of FMN was shown to work in Escherichia coli and Saccharomyces cerevisiae cells and could be performed in vitro, rendering the "Flavin-Tag"method a powerful tool for the selective decoration of proteins with a biocompatible redox-Active fluorescent chromophore.
- Subjects :
- Saccharomyces cerevisiae Proteins
Fluorophore
Stereochemistry
Saccharomyces cerevisiae
Biomedical Engineering
Pharmaceutical Science
Bioengineering
Peptide
Flavin group
chemistry.chemical_compound
Flavins
Escherichia coli
Transferase
heterocyclic compounds
Phosphorylation
Fluorescent Dyes
Pharmacology
chemistry.chemical_classification
Staining and Labeling
biology
Escherichia coli Proteins
Organic Chemistry
Proteins
biology.organism_classification
Fluorescence
chemistry
Covalent bond
Target protein
Biotechnology
Subjects
Details
- Language :
- English
- ISSN :
- 10431802
- Volume :
- 32
- Issue :
- 8
- Database :
- OpenAIRE
- Journal :
- BIOCONJUGATE CHEMISTRY
- Accession number :
- edsair.doi.dedup.....8d4952611d4cfe75043853db2d61b34b