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Related Experiment Video

Updated: Jan 13, 2026

Determination of Tripartite Interaction between Two Monomers of a MADS-box Transcription Factor and a Calcium Sensor Protein by BiFC-FRET-FLIM Assay
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FRET-FLIM: Unveiling Transcription Factor Interactions in Plants.

María Florencia Perotti1, Carlos Sánchez-Gómez1, Carmen Martin-Pizarro2

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This study details a Förster resonance energy transfer combined with fluorescence lifetime imaging microscopy (FRET-FLIM) protocol for visualizing protein-protein interactions in cells. The method uses fluorescent tags to detect interactions between transcription factors in vivo.

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biophysics

Background:

  • Gene regulation depends on transcription factors (TFs) interacting dynamically within cells.
  • Assaying these protein-protein interactions in vivo is essential for understanding gene expression.
  • Förster resonance energy transfer (FRET) combined with fluorescence lifetime imaging microscopy (FLIM) is a powerful technique for in vivo interaction studies.

Purpose of the Study:

  • To present a detailed protocol for acquiring and analyzing FRET-FLIM data.
  • To demonstrate the application of FRET-FLIM for studying transcription factor interactions.
  • To provide a user-friendly method for in vivo protein-protein interaction analysis.

Main Methods:

  • Utilized Förster resonance energy transfer combined with fluorescence lifetime imaging microscopy (FRET-FLIM).
  • Labeled target proteins with fluorescent tags for FRET-FLIM analysis.
  • Employed the Leica STELLARIS 8 FALCON FLIM Microscope system for data acquisition and analysis.

Main Results:

  • Successfully acquired and analyzed FRET-FLIM data to detect protein-protein interactions.
  • Demonstrated the method's efficacy using two interacting transcription factors as a model system.
  • Showcased the reduction in donor fluorophore lifetime as direct evidence of physical interaction.

Conclusions:

  • FRET-FLIM is a robust and quantitative method for studying protein-protein interactions in vivo.
  • The presented protocol offers a simplified approach to FRET-FLIM data acquisition and analysis.
  • This technique is crucial for elucidating the mechanisms of gene regulation mediated by protein complexes.