ArticleProceedings of the National Academy of Sciences of the United States of America2004
EosFP, a fluorescent marker protein with UV-inducible green-to-red fluorescence conversion.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 278 papers.
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278 citing papers in PubMed.
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- Polar localization and local translation of RHO-RELATED PROTEIN FROM PLANTS2 mRNAs promote root hair growth in Arabidopsis.The Plant cell · 2024Article
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- Structural Heterogeneity in a Phototransformable Fluorescent Protein Impacts its Photochemical Properties.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
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- Engineering and Characterization of 3-Aminotyrosine-Derived Red Fluorescent Variants of Circularly Permutated Green Fluorescent Protein.Biosensors · 2024Article
- Using ER-Targeted Photoconvertible Fluorescent Proteins in Living Plant Cells.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Organelle Interactions in Plant Cells.Results and problems in cell differentiation · 2024Review
- Variable-Angle Epifluorescence Microscopy for Single-Particle Tracking in the Plant ER.Methods in molecular biology (Clifton, N.J.) · 2024Article
218 more citing papers are in PubMed but not listed here.
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8 authors.
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No grant is acknowledged in the PubMed record.
Abstract
A gene encoding a fluorescent protein from the stony coral Lobophyllia hemprichii has been cloned in Escherichia coli and characterized by biochemical and biophysical methods. The protein, which we named EosFP, emits strong green fluorescence (516 nm) that changes to red (581 nm) upon near-UV irradiation at approximately 390 nm because of a photo-induced modification involving a break in the peptide backbone next to the chromophore. Single-molecule fluorescence spectroscopy shows that the wild type of EosFP is tetrameric, with strong Forster resonance coupling among the individual fluorophores. We succeeded in breaking up the tetramer into AB and AC subunit dimers by introducing the single point mutations V123T and T158H, respectively, and the combination of both mutations yielded functional monomers. Fusion constructs with a variety of proteins were prepared and expressed in human cells, showing that normal biological functions were retained. The possibility to locally change the emission wavelength by focused UV light makes EosFP a superb marker for experiments aimed at tracking the movements of biomolecules within the living cell.
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