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Related Experiment Video

Updated: Jul 5, 2026

Bimolecular Fluorescence Complementation
08:54

Bimolecular Fluorescence Complementation

Published on: April 15, 2011

Development and implementation of split-GFP-based bimolecular fluorescence complementation (BiFC) assays in yeast.

Emma Barnard1, Neil V McFerran, Alan Trudgett

  • 1School of Biological Sciences, Queen's University Belfast, Medical Biology Centre, 97 Lisburn Road, Belfast BT9 7BL, Northern Ireland, UK.

Biochemical Society Transactions
|May 17, 2008
PubMed
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Bimolecular fluorescence complementation (BiFC) using split-green fluorescent protein (GFP) allows visualization of protein interactions in living yeast cells. This genomic-level assay accurately detects interactions in various cellular locations.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Protein-protein interactions are crucial for cellular functions.
  • Bimolecular fluorescence complementation (BiFC) is a technique to study these interactions.
  • Existing BiFC methods may have limitations in specific model organisms.

Purpose of the Study:

  • To develop and validate a novel split-green fluorescent protein (GFP)-based BiFC assay.
  • To enable the study of protein interactions at the genomic level in Saccharomyces cerevisiae.
  • To assess the assay's capability in detecting interactions across different subcellular compartments.

Main Methods:

  • Fusion of non-fluorescent GFP fragments to interacting proteins in Saccharomyces cerevisiae.
  • Genomic integration of BiFC constructs for endogenous protein expression levels.

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Single Molecule Fluorescence In Situ Hybridization (smFISH) Analysis in Budding Yeast Vegetative Growth and Meiosis
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Last Updated: Jul 5, 2026

Bimolecular Fluorescence Complementation
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Bimolecular Fluorescence Complementation

Published on: April 15, 2011

Detection of Protein Interactions in Plant using a Gateway Compatible Bimolecular Fluorescence Complementation (BiFC) System
08:21

Detection of Protein Interactions in Plant using a Gateway Compatible Bimolecular Fluorescence Complementation (BiFC) System

Published on: September 16, 2011

Single Molecule Fluorescence In Situ Hybridization (smFISH) Analysis in Budding Yeast Vegetative Growth and Meiosis
09:28

Single Molecule Fluorescence In Situ Hybridization (smFISH) Analysis in Budding Yeast Vegetative Growth and Meiosis

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  • Detection of fluorescence complementation in living yeast cells.
  • Main Results:

    • Successful development of a split-GFP BiFC system for yeast.
    • Demonstrated detection of protein interactions in the cytoplasm, mitochondria, and nucleus.
    • Yeast proteins expressed at wild-type levels due to genomic modifications.

    Conclusions:

    • The developed BiFC assay is a valuable tool for studying protein-protein interactions in yeast.
    • The system provides insights into interaction localization within the cell.
    • This method enhances the investigation of protein dynamics in Saccharomyces cerevisiae.