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Related Concept Videos

Protein Networks02:26

Protein Networks

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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,...
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Related Experiment Video

Updated: Oct 23, 2025

In Vivo Proximity Biotinylation for Protein Interaction Studies in Paramecium tetraurelia
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In Vivo Proximity Biotinylation for Protein Interaction Studies in Paramecium tetraurelia

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Off-the-shelf proximity biotinylation for interaction proteomics.

Irene Santos-Barriopedro1, Guido van Mierlo2, Michiel Vermeulen3

  • 1Department of Molecular Biology, Faculty of Science, Radboud Institute for Molecular Life Sciences, Oncode Institute, Radboud University Nijmegen, Nijmegen, The Netherlands.

Nature Communications
|August 19, 2021
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Summary

A new ProtA-Turbo enzyme enables proximity biotinylation without genetic engineering. This method revealed FLYWCH1 interactions with H3K9me3-marked centromeres, advancing cellular research.

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Split-BioID &#8212; Proteomic Analysis of Context-specific Protein Complexes in Their Native Cellular Environment
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Split-BioID — Proteomic Analysis of Context-specific Protein Complexes in Their Native Cellular Environment

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Proximity biotinylation is crucial for mapping protein interactions but often requires genetic manipulation.
  • CRISPR-based methods are a bottleneck for studying primary cells or complex biological systems.

Purpose of the Study:

  • To develop a versatile proximity biotinylation method independent of genetic engineering.
  • To investigate protein interactions and post-translational modifications in native cellular environments.

Main Methods:

  • Fusion of Protein A with the TurboID proximity biotinylation enzyme (ProtA-Turbo).
  • Antibody-based targeting of ProtA-Turbo to specific proteins or modifications (e.g., Emerin, H3K9me3, BRG1) after cell permeabilization.
  • Biotinylation of proximal proteins, followed by enrichment and mass spectrometry identification.

Main Results:

  • Successful proximity biotinylation of proteins associated with targeted baits.
  • Identification of novel interactions, including FLYWCH1 with H3K9me3-marked (peri)centromeres.
  • Demonstration of the workflow's applicability in primary cells.

Conclusions:

  • ProtA-Turbo offers an accessible off-the-shelf solution for proximity biotinylation.
  • This method facilitates in vivo studies of protein cooperation, cellular homeostasis, and disease mechanisms.
  • The findings highlight FLYWCH1's role in centromeric regulation.