ArticleScientific reports2015
An Efficient Site-Specific Method for Irreversible Covalent Labeling of Proteins with a Fluorophore.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 21 citations in OpenAlex.
- Chemical Conjugation to Less Targeted Proteinogenic Amino Acids.Chembiochem : a European journal of chemical biology · 2022Review
- Observing Protein One-Dimensional Sliding: Methodology and Biological Significance.Biomolecules · 2021Review
- A versatile soluble siglec scaffold for sensitive and quantitative detection of glycan ligands.Nature communications · 2020Article
- The Pictet-Spengler Reaction Updates Its Habits.Molecules (Basel, Switzerland) · 2020Review
- MutL sliding clamps coordinate exonuclease-independent Escherichia coli mismatch repair.Nature communications · 2019Article
- Investigating supramolecular systems using Förster resonance energy transfer.Chemical Society reviews · 2018Review
- MutS homolog sliding clamps shield the DNA from binding proteins.The Journal of biological chemistry · 2018Article
- Expression and purification of nuclease-free protocatechuate 3,4-dioxygenase for prolonged single-molecule fluorescence imaging.Analytical biochemistry · 2018Article
- Cascading MutS and MutL sliding clamps control DNA diffusion to activate mismatch repair.Nature · 2016Article
- Site-Specific Tandem Knoevenagel Condensation-Michael Addition To Generate Antibody-Drug Conjugates.ACS medicinal chemistry letters · 2016Article
- Quantifying the Assembly of Multicomponent Molecular Machines by Single-Molecule Total Internal Reflection Fluorescence Microscopy.Methods in enzymology · 2016Article
Corrections and comments
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Authors and funding
11 authors at 4 institutions in 2 countries.
Funding
Abstract
Fluorophore labeling of proteins while preserving native functions is essential for bulk Förster resonance energy transfer (FRET) interaction and single molecule imaging analysis. Here we describe a versatile, efficient, specific, irreversible, gentle and low-cost method for labeling proteins with fluorophores that appears substantially more robust than a similar but chemically distinct procedure. The method employs the controlled enzymatic conversion of a central Cys to a reactive formylglycine (fGly) aldehyde within a six amino acid Formylglycine Generating Enzyme (FGE) recognition sequence in vitro. The fluorophore is then irreversibly linked to the fGly residue using a Hydrazinyl-Iso-Pictet-Spengler (HIPS) ligation reaction. We demonstrate the robust large-scale fluorophore labeling and purification of E.coli (Ec) mismatch repair (MMR) components. Fluorophore labeling did not alter the native functions of these MMR proteins in vitro or in singulo. Because the FGE recognition sequence is easily portable, FGE-HIPS fluorophore-labeling may be easily extended to other proteins.
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Registered trials
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