2C-BioID: An Advanced Two Component BioID System for Precision Mapping of Protein Interactomes

Overview

Journal iScience

Publisher Cell Press

Date 2018 Dec 1

PMID 30500481

Citations 23

Authors

Alexandre Chojnowski

Radoslaw M Sobota

Peh Fern Ong

Wei Xie

Xianrong Wong

Oliver Dreesen

Brian Burke

Colin L Stewart

Affiliations

Soon will be listed here.

Abstract

The modulation of protein-protein interactions (PPIs) is an essential regulatory activity defining diverse cell functions in development and disease. BioID is an unbiased proximity-dependent biotinylation method making use of a biotin-protein ligase fused to a protein of interest and has become an important tool for mapping of PPIs within cellular contexts. We devised an advanced method, 2C-BioID, in which the biotin-protein ligase is kept separate from the protein of interest, until the two are induced to associate by the addition of a dimerizing agent. As proof of principle, we compared the interactomes of lamina-associated polypeptide 2β (LAP2β) with those of lamins A and C, using 2C- and conventional BioID. 2C-BioID greatly enhanced data robustness by facilitating the in silico elimination of non-specific interactors as well as overcoming the problems associated with aberrant protein localization. 2C-BioID therefore significantly strengthens the specificity and reliability of BioID-based interactome analysis, by the more stringent exclusion of false-positives and more efficient intracellular targeting.

Citing Articles

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Analyzing Protein Interactions by MAC-Tag Approaches.

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Chemical and Biological Strategies for Profiling Protein-Protein Interactions in Living Cells.

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