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Protein Dynamics in Living Cells

Protein Dynamics in Living Cells

Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...

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Related Experiment Video

Updated: Feb 17, 2026

Co-expression of Multiple Chimeric Fluorescent Fusion Proteins in an Efficient Way in Plants

Co-expression of Multiple Chimeric Fluorescent Fusion Proteins in an Efficient Way in Plants

Published on: July 1, 2018

Simultaneous visualization of two protein complexes in a single plant cell using multicolor fluorescence

Yutaka Kodama¹, Masamitsu Wada

¹Division of Photobiology, National Institute for Basic Biology, Okazaki, 444-8585, Japan.

Plant Molecular Biology

|February 17, 2009

Summary

This summary is machine-generated.

This study introduces multicolor Bimolecular Fluorescence Complementation (BiFC) for plant cells, enabling simultaneous visualization of two protein complexes. Researchers successfully used cyan, yellow, green, and red fluorescent protein fragments for dual-color imaging in plants.

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

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Last Updated: Feb 17, 2026

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

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

Published on: September 16, 2011

Area of Science:

Molecular Biology
Plant Science
Biochemistry

Background:

Bimolecular fluorescence complementation (BiFC) analyzes protein-protein interactions in vivo.
Multicolor BiFC using green fluorescent protein (GFP) variants has been established in animal cells.
Visualizing multiple protein interactions simultaneously in plants requires advanced molecular tools.

Purpose of the Study:

To develop and validate a multicolor BiFC strategy for simultaneous visualization of two protein complexes in plant cells.
To expand the utility of BiFC in plant research by incorporating a red fluorescent protein.
To enable dual-color imaging of protein interactions within a single plant cell.

Main Methods:

Utilized fragments of cyan (CFP), yellow (YFP), green (GFP), and red (DsRed-Monomer) fluorescent proteins for BiFC assays.
Constructed and tested various combinations of fluorescent protein fragments to identify functional BiFC pairs.
Applied identified BiFC pairs to achieve simultaneous visualization of two protein complexes in plant cells.

Main Results:

Identified nine functional BiFC complexes using CFP, YFP, and GFP fragments.
Confirmed one functional BiFC complex using DsRed-Monomer fragments.
Demonstrated successful simultaneous visualization of two protein complexes in plant cells using cyan/red, green/red, or yellow/red BiFC pairs.

Conclusions:

A novel multicolor BiFC system has been established for plant cells.
This method allows for the simultaneous observation of two distinct protein-protein interactions.
The developed BiFC strategy enhances the capability for studying complex molecular interactions in plants.