Use of BioID to detect protein-protein interactions
DOI:
https://doi.org/10.14288/cjur.v3i1.201783Abstract
Proximity-dependent biotin identification (BioID) is a novel approach to identify protein-protein interactions (PPIs) in a natural cellular environment. BioID exploits a mutant form of a biotin protein ligase found in Escherichia coli, BirA*, that promiscuously catalyses biotinylation of proteins in close-proximity of the enzyme. Biotinylated proteins are then purified with conventional methods. BioID has been shown to overcome many of the limitations faced by traditional PPI techniques, such as co-immunoprecipitation, proximity ligation assays and yeast two-hybrid systems. The main advantages of BioID as compared to these methods include high sensitivity and spatial resolution, preservation of physiologically- relevant conditions, and detection of weak or transient interactions. Despite some inherent limitations, BioID remains a promising PPI technique and has led to more advanced methods, such as BioID2 and split-BioID.
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