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Related Experiment Video

Updated: Jan 13, 2026

TurboID-Based Proximity Labeling for In Planta Identification of Protein-Protein Interaction Networks
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TurboID-Based Proximity Labeling in Plants.

Chaonan Shi1, Huang Tan2, Rosa Lozano-Durán3

  • 1Department of Plant Biochemistry, Centre for Plant Molecular Biology (ZMBP), Eberhard Karls University, Tübingen, Germany. chaonan.shi@uni-tuebingen.de.

Methods in Molecular Biology (Clifton, N.J.)
|January 10, 2026
PubMed
Summary

This chapter details a TurboID proximity labeling protocol for identifying plant protein interactions. It guides researchers from creating fusion proteins to analyzing results using the Ti-TAN plasmid collection.

Keywords:
Nicotiana benthamianaProtein complexesProtein-protein interactionsProximal proteomeProximity labelingProxiomeTurboID

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Plant Science

Background:

  • Proximity labeling (PL) techniques are vital for studying protein-protein interactions in living organisms.
  • Understanding protein associations is crucial for deciphering cellular processes in plants.

Purpose of the Study:

  • To present a detailed, step-by-step protocol for TurboID-based proximity labeling in plants.
  • To enable the comprehensive definition of a protein's "proxiome" (interacting partners) in a plant context.

Main Methods:

  • Utilizing the TurboID enzyme for proximity-dependent biotinylation.
  • Employing the publicly available Ti-TAN plasmid collection for generating fusion proteins.
  • A comprehensive workflow from fusion protein generation to data analysis.

Main Results:

  • The protocol facilitates the identification of proximal proteins to a protein of interest.
  • Successful application of TurboID-based PL for mapping plant protein interactomes.
  • The Ti-TAN plasmid collection simplifies the experimental setup.

Conclusions:

  • This TurboID-based proximity labeling protocol provides a robust method for plant interactome studies.
  • The presented workflow empowers researchers to investigate protein associations in vivo.
  • This approach enhances the understanding of plant molecular mechanisms.