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Related Concept Videos

Super-resolution Fluorescence Microscopy01:37

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Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
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Related Experiment Video

Updated: Nov 15, 2025

Bimolecular Fluorescence Complementation
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Bimolecular Fluorescence Complementation

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Super-resolution Microscopy-based Bimolecular Fluorescence Complementation to Study Protein Complex Assembly and

Jingjing Chen1, Zulin Yu1, Jay R Unruh1

  • 1Stowers Institute for Medical Research, Kansas City, MO 64110, USA.

Bio-Protocol
|March 3, 2021
PubMed
Summary
This summary is machine-generated.

We developed a super-resolution microscopy method combining HyVolution and bimolecular fluorescence complementation (SRM-BiFC) to visualize protein interactions in live cells. This technique provides sub-diffraction resolution, aiding the study of complex biological assembly processes.

Keywords:
BiFCHyvolutionProtein complex assemblySIMSuper-resolution microscopyYeast

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Photoactivated Localization Microscopy with Bimolecular Fluorescence Complementation BiFC-PALM
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Area of Science:

  • Cell Biology
  • Biophysics
  • Microscopy

Background:

  • Studying macromolecular complex assembly in vivo requires spatial and temporal binding information.
  • Existing methods often lack resolution or struggle with multi-color live-cell imaging.
  • Super-resolution microscopy advances offer potential but face technical challenges.

Purpose of the Study:

  • To develop a novel super-resolution assay for visualizing protein-protein interactions in vivo.
  • To overcome limitations of existing techniques in spatial and temporal resolution.
  • To apply the assay to understand the assembly of the Saccharomyces cerevisiae spindle pole body.

Main Methods:

  • Utilized HyVolution super-resolution microscopy with computational deconvolution for 140 nm resolution.
  • Developed a super-resolution bimolecular fluorescence complementation (SRM-BiFC) assay.
  • Successfully imaged three colors, including spectrally overlapping fluorescent proteins, in live and fixed samples.

Main Results:

  • Achieved 140 nm resolution in live and fixed samples using HyVolution.
  • Demonstrated the capability of SRM-BiFC to visualize direct protein-protein interactions in vivo at sub-diffraction resolution.
  • Provided new insights into the ordered assembly of the Saccharomyces cerevisiae spindle pole body.

Conclusions:

  • SRM-BiFC is a powerful new tool for examining direct protein subunit interactions in vivo.
  • The method offers sub-diffraction resolution for studying complex biological assemblies.
  • This technique enhances our understanding of dynamic cellular processes like the SPB assembly.