UNIT 19.23 BioID: A Screen for Protein-Protein Interactions
Published Online: 5 NOV 2013
Copyright © 2013 John Wiley & Sons, Inc. All rights reserved.
Lab Protocol Title
Current Protocols in Protein Science
How to Cite
Roux, K. J., Kim, D. I. and Burke, B. 2013. BioID: A Screen for Protein-Protein Interactions. Current Protocols in Protein Science. 74:19.23:19.23.1–19.23.14.
- Published Online: 5 NOV 2013
BioID is a unique method to screen for physiologically relevant protein interactions that occur in living cells. This technique harnesses a promiscuous biotin ligase to biotinylate proteins based on proximity. The ligase is fused to a protein of interest and expressed in cells, where it biotinylates proximal endogenous proteins. Because it is a rare protein modification in nature, biotinylation of these endogenous proteins by BioID fusion proteins enables their selective isolation and identification with standard biotin-affinity capture. Proteins identified by BioID are candidate interactors for the protein of interest. BioID can be applied to insoluble proteins, can identify weak and/or transient interactions, and is amenable to temporal regulation. Initially applied to mammalian cells, BioID has potential application in a variety of cell types from diverse species. Curr. Protoc. Protein Sci. 74:19.23.1-19.23.14. © 2013 by John Wiley & Sons, Inc.
- proximity-dependent labeling;
- protein-protein interaction;