Proteomics

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


ABSTRACT: The use of proximity-dependent biotinylation assays coupled to mass spectrometry (PDB-MS) has changed the field of protein-protein interactions (PPI) studies. Yet, despite the recurrent and successful use of BioID-based PPI 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 interacting proteins in their natural cellular environment by using TurboID, a recently described version of the BirA biotin ligase. Using the protein arginine methyltransferase Rmt3 and the RNA exosome subunits, Rrp6 and Dis3, the application of PDB-MS in yeast by using TurboID was able to recover protein-protein interactions previously identified using other biochemical approaches and provided complementary information for a given protein bait. The development of a rapid and effective PDB assay that can systematically analyze PPIs in living yeast cells opens the way for large-scale proteomics studies in this powerful model organism.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Schizosaccharomyces Pombe 927

SUBMITTER: Danny Bergeron  

LAB HEAD: Francois Bachand

PROVIDER: PXD013183 | Pride | 2019-05-16

REPOSITORIES: Pride

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Publications

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

Larochelle Marc M   Bergeron Danny D   Arcand Bruno B   Bachand François F  

Journal of cell science 20190531 11


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 interacting proteins in their natural cellular environment by using Tu  ...[more]

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