Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Tagging and Fusion Proteins01:24

Tagging and Fusion Proteins

Proteins are involved in several cellular processes and biochemical reactions. Analyzing a specific protein of interest requires it to be isolated from the other proteins in the cell. This is achieved by overexpressing the specific gene in a suitable host to produce large quantities of the target protein. A tag or label is recombined with the gene to produce a fusion protein containing the target protein and the tag. The tags on these fusion proteins can then be used for easy detection and...
Protein Networks02:26

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

miR-217/Mafb Axis Involve in High Glucose-Induced β-TC-tet Cell Damage Via Regulating NF-κB Signaling Pathway.

Biochemical genetics·2020
Same author

Fasciclin-like arabinogalactan gene family in Nicotiana benthamiana: genome-wide identification, classification and expression in response to pathogens.

BMC plant biology·2020
Same author

Discovery of Two Novel Negeviruses in a Dungfly Collected from the Arctic.

Viruses·2020
Same author

The OsGSK2 Kinase Integrates Brassinosteroid and Jasmonic Acid Signaling by Interacting with OsJAZ4.

The Plant cell·2020
Same author

Interleukin (IL)-33: an orchestrator of immunity from host defence to tissue homeostasis.

Clinical & translational immunology·2020
Same author

Higher Iodine Concentration Enables Radiation Dose Reduction in Coronary CT Angiography.

Academic radiology·2020
Same journal

Mapping the 3D Chromosome Organization of a Biosynthetic Gene Cluster by Capture Hi-C (CHi-C).

Methods in molecular biology (Clifton, N.J.)·2026
Same journal

Mapping the 3D Chromosome Organization of Streptomyces by Hi-C.

Methods in molecular biology (Clifton, N.J.)·2026
Same journal

CUT&Tag Epigenomic Profiling of Biosynthetic Gene Clusters in Arabidopsis thaliana.

Methods in molecular biology (Clifton, N.J.)·2026
Same journal

Rhizobium rhizogenes-Mediated Hairy Root Transformation Protocol for Lotus japonicus and Other Legumes.

Methods in molecular biology (Clifton, N.J.)·2026
Same journal

Characterization of Bioactive Saponins from Sea Cucumbers.

Methods in molecular biology (Clifton, N.J.)·2026
Same journal

Methods for Functional Validation of Terpenoid Metabolic Clusters in Nicotiana benthamiana and Aspergillus oryzae.

Methods in molecular biology (Clifton, N.J.)·2026
See all related articles

Related Experiment Video

Updated: May 15, 2026

TurboID-Based Proximity Labeling for In Planta Identification of Protein-Protein Interaction Networks
07:02

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

Published on: May 17, 2020

A TurboID-Based Protocol for Efficient Interacting Proteins Identification Using Proximity Tagging Technology.

Xinxin Fang1, Jianping Chen1, Fei Yan2

  • 1State Key Laboratory for Quality and Safety of Agro-products, Key Laboratory of Biotechnology in Plant Protection of MARA, Key Laboratory of Green Plant Protection of Zhejiang Province, Institute of Plant Virology, Ningbo University, Ningbo, China.

Methods in Molecular Biology (Clifton, N.J.)
|May 13, 2026
PubMed
Summary
This summary is machine-generated.

This study details a TurboID-based proximity labeling protocol to map protein-protein interactions (PPIs). This method efficiently identifies interacting proteins in living cells, overcoming limitations of traditional techniques.

Keywords:
Nicotiana benthamianaProtein–protein interactionTurboID

More Related Videos

Identification of Protein Interacting Partners Using Tandem Affinity Purification
10:02

Identification of Protein Interacting Partners Using Tandem Affinity Purification

Published on: February 25, 2012

A Protocol for the Identification of Protein-protein Interactions Based on 15N Metabolic Labeling, Immunoprecipitation, Quantitative Mass Spectrometry and Affinity Modulation
14:44

A Protocol for the Identification of Protein-protein Interactions Based on 15N Metabolic Labeling, Immunoprecipitation, Quantitative Mass Spectrometry and Affinity Modulation

Published on: September 24, 2012

Related Experiment Videos

Last Updated: May 15, 2026

TurboID-Based Proximity Labeling for In Planta Identification of Protein-Protein Interaction Networks
07:02

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

Published on: May 17, 2020

Identification of Protein Interacting Partners Using Tandem Affinity Purification
10:02

Identification of Protein Interacting Partners Using Tandem Affinity Purification

Published on: February 25, 2012

A Protocol for the Identification of Protein-protein Interactions Based on 15N Metabolic Labeling, Immunoprecipitation, Quantitative Mass Spectrometry and Affinity Modulation
14:44

A Protocol for the Identification of Protein-protein Interactions Based on 15N Metabolic Labeling, Immunoprecipitation, Quantitative Mass Spectrometry and Affinity Modulation

Published on: September 24, 2012

Area of Science:

  • Molecular Biology
  • Cellular Biology
  • Biochemistry

Background:

  • Protein-protein interactions (PPIs) are crucial for cellular signaling and biological processes.
  • Conventional PPI identification methods like yeast two-hybrid and co-immunoprecipitation have limitations in spatiotemporal resolution and detecting transient interactions.
  • Proximity-dependent biotinylation (PDB) coupled with mass spectrometry (MS) offers a powerful approach to map the spatial proteome.

Purpose of the Study:

  • To provide a detailed protocol for TurboID-based proximity labeling.
  • To identify potential interacting proteins of a target protein of interest.
  • To leverage the high catalytic efficiency of TurboID for rapid protein interaction mapping.

Main Methods:

  • Utilizing TurboID, an engineered biotin ligase with high catalytic efficiency.
  • Performing proximity labeling experiments in living cells.
  • Employing mass spectrometry (MS) for the identification of biotinylated proteins.

Main Results:

  • TurboID enables rapid biotinylation of proximal proteins within minutes.
  • The protocol facilitates the identification of a target protein's interacting partners.
  • This technique enhances the mapping of the spatial proteome.

Conclusions:

  • TurboID-based proximity labeling is an efficient method for mapping protein-protein interactions.
  • This protocol overcomes limitations of traditional PPI identification techniques.
  • The method is valuable for studying dynamic cellular processes and signaling pathways.