ArticleScientific reports2017
Characterization of a spectrally diverse set of fluorescent proteins as FRET acceptors for mTurquoise2.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.
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Who cites it
60 citing papers in PubMed.
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- Development of three-colour FRET cascade for force sensing of the putative RIAM-vinculin interaction in fibroblasts.Communications chemistry · 2025Article
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- Different mCherry isoforms show distinct photophysical properties in FRET tandem constructs.Frontiers in bioengineering and biotechnology · 2025Article
- FRET-FLIM for the Study of Protein-Protein Interactions Underpinning Mitosis Checkpoints.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Direct observation of subunit rotation during DNA strand exchange by serine recombinases.Nature communications · 2024Article
- Decoding Insulin Secretory Granule Maturation Using Genetically Encoded pH Sensors.ACS sensors · 2024Article
- Shining a light on the impact of antifungals onAntimicrobial agents and chemotherapy · 2024Article
- MYC phase separation selectively modulates the transcriptome.Nature structural & molecular biology · 2024Article
- Transcription factor dynamics, oscillation, and functions in human enteroendocrine cell differentiation.Cell stem cell · 2024Article
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6 authors.
Funding
Abstract
The performance of Förster Resonance Energy Transfer (FRET) biosensors depends on brightness and photostability, which are dependent on the characteristics of the fluorescent proteins that are employed. Yellow fluorescent protein (YFP) is often used as an acceptor but YFP is prone to photobleaching and pH changes. In this study, we evaluated the properties of a diverse set of acceptor fluorescent proteins in combination with the optimized CFP variant mTurquoise2 as the donor. To determine the theoretical performance of acceptors, the Förster radius was determined. The practical performance was determined by measuring FRET efficiency and photostability of tandem fusion proteins in mammalian cells. Our results show that mNeonGreen is the most efficient acceptor for mTurquoise2 and that the photostability is better than SYFP2. The non-fluorescent YFP variant sREACh is an efficient acceptor, which is useful in lifetime-based FRET experiments. Among the orange and red fluorescent proteins, mCherry and mScarlet-I are the best performing acceptors. Several new pairs were applied in a multimolecular FRET based sensor for detecting activation of a heterotrimeric G-protein by G-protein coupled receptors. Overall, the sensor with mNeonGreen as acceptor and mTurquoise2 as donor showed the highest dynamic range in ratiometric FRET imaging experiments with the G-protein sensor.
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