An interaction is inferred when a bait-enzyme fusion protein selectively modifies a vicinal protein with a diffusible reactive product, followed by affinity capture of the modified protein and identification by mass spectrometric methods.

Publication

Proximity-dependent biotinylation mediated by TurboID to identify protein-protein interaction networks in yeast.

Larochelle M, Bergeron D, Arcand B, Bachand F

The use of proximity-dependent biotinylation assays coupled to mass spectrometry (PDB-MS) has changed the field of protein-protein interaction studies. However, despite the recurrent and successful use of BioID-based protein-protein interactions screening in mammalian cells, the implementation of PDB-MS in yeast has not been effective. Here, we report a simple and rapid approach in yeast to effectively screen for proximal and ... [more]

J Cell Sci Dec. 31, 2018; 132(11); [Pubmed: 31064814]

Throughput

Low Throughput

Additional Notes

Proximity-dependent biotinylation assay coupled to mass spectrometry

Curated By

BioGRID

Interaction Summary

RMT3

Gene Ontology Biological Process

Gene Ontology Molecular Function

methyltransferase activity [IDA]protein binding [IPI]protein-arginine N-methyltransferase activity [IMP]ribosome binding [IDA]

Gene Ontology Cellular Component

HRS1