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BioID: A Proximity-Dependent Labeling Approach in Proteomics Study: Methods and Protocols
Peipei Li; Yuan Meng; Li Wang; Li-jun Di
Source PublicationFunctional Proteomics
PublisherHumana Press, New York, NY

Biological activities are mainly executed by proteins and in most of the occasions these activities are accomplished by protein complexes or through protein–protein interactions (PPI). So it is critical to reveal how the protein complexes are organized and demonstrate the PPIs involved in the biological processes. In addition to the traditional biochemical approaches, proximity-dependent labeling (PDL) has recently been proposed to identify the interacting partners of a given protein. PDL requires the fusion expression of the target protein with an enzyme which catalyzes the attachment of a reactive molecule to the interacting partners in a distance-dependent manner. Further analysis of all the proteins that are modified by the reactive molecule discloses the identity of these proteins which are presumed to be interacting partners of the target protein. BioID is one of those representative PDL methods with the most widely applications. The enzyme used in BioID is a biotin ligase BirA which catalyzes the biotinylation of target protein with the presence of biotin. Through streptavidin-mediated pull-down and mass spectrometry analysis, the interacting protein candidates of a given protein can be obtained.

KeywordBioid Proximity-dependent Labeling Protein–protein Interactions
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Document TypeBook chapter
CollectionFaculty of Health Sciences
AffiliationFaculty of Health Sciences, Cancer CenterUniversity of MacauMacauChina
First Author AffilicationFaculty of Health Sciences
Recommended Citation
GB/T 7714
Peipei Li,Yuan Meng,Li Wang,et al. BioID: A Proximity-Dependent Labeling Approach in Proteomics Study: Methods and Protocols:Humana Press, New York, NY,2018:143-151.
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