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Bimolecular Fluorescence Complementation
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A split fluorescent reporter with rapid and reversible complementation.

Alison G Tebo1, Arnaud Gautier2

  • 1PASTEUR, Department of Chemistry, École Normale Supérieure, PSL University, Sorbonne University, CNRS, 75005, Paris, France.

Nature Communications
|June 29, 2019
PubMed
Summary

Researchers developed splitFAST, a novel fluorescence system, to visualize protein interactions in real-time within living cells. This tool enables tracking the dynamic formation and breakdown of protein assemblies.

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Protein-protein interactions are crucial for cellular functions, including metabolic and signaling pathways.
  • Visualizing these interactions in real-time within living cells is essential for understanding cellular processes.

Purpose of the Study:

  • To develop a novel fluorescence complementation system for visualizing transient protein-protein interactions in living cells.
  • To engineer a system capable of real-time monitoring of protein assembly dynamics.

Main Methods:

  • Development of splitFAST, a split version of the FAST (Fluorescence-Activating and absorption-Shifting Tag) reporter.
  • Utilizing the specific and reversible binding of FAST to hydroxybenzylidene rhodanine (HBR) analogs.
  • Applying splitFAST for the visualization of protein assembly formation and dissociation in living cells.

Main Results:

  • Demonstrated the successful development of splitFAST, a fluorescence complementation system.
  • Showcased rapid and reversible complementation of splitFAST.
  • Enabled real-time visualization of both the formation and dissociation of protein assemblies.

Conclusions:

  • splitFAST is an effective tool for visualizing transient protein-protein interactions in living cells.
  • The system allows for real-time monitoring of dynamic protein assembly processes.
  • splitFAST offers a valuable method for studying cellular pathways and organismal systems.