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Updated: Jul 23, 2025
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TurboID-Based Proximity Labeling for In Planta Identification of Protein-Protein Interaction Networks
Published on: May 17, 2020
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Cataloguing Protein Complexes In Planta Using TurboID-Catalyzed Proximity Labeling
Lore Gryffroy1,2,3, Joren De Ryck1,2,3, Veronique Jonckheere3
1Department of Plant Biotechnology and Bioinformatics, Ghent University, Ghent, Belgium.
Methods in Molecular Biology (Clifton, N.J.)
|July 14, 2023
Summary
We detail how to use proximity-dependent biotinylation (BioID) with mass spectrometry (MS) to map protein interactions in tomato hairy root cultures. This method helps understand complex protein functions in plants.
Area of Science:
- Plant molecular biology
- Biochemistry
- Proteomics
Background:
- Understanding protein-protein interactions is key to elucidating protein functions.
- Proximity-dependent biotinylation (BioID) coupled with mass spectrometry (MS) is a powerful technique for characterizing protein complexes.
- This method has been successfully applied across various plant models.
Purpose of the Study:
- To describe the application of BioID in tomato hairy root cultures.
- To provide a detailed protocol for analyzing BioID-MS data in this plant system.
- To facilitate the study of protein complex dynamics in tomato.
Main Methods:
- Utilizing BioID technology in tomato hairy root cultures.
- Employing mass spectrometry (MS) for the identification of biotinylated proteins.
- Developing and detailing data analysis pipelines for BioID-MS output.
Main Results:
- Successful implementation of BioID in tomato hairy root systems.
- Generation of comprehensive datasets of protein interactions.
- Establishment of a workflow for robust data interpretation.
Conclusions:
- BioID is an effective method for mapping protein-protein interactions in tomato.
- The described protocol enables detailed analysis of protein complexes in plant research.
- This approach advances the understanding of protein function in agriculturally important species.
