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- W2944714048 abstract "The use of proximity-dependent biotinylation assays coupled to mass spectrometry (PDB-MS) has changed the field of protein-protein interaction studies. Yet, 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 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 new complementary information for a given protein bait. The development of a rapid and effective PDB assay that can systematically analyze protein-protein interactions in living yeast cells opens the way for large-scale proteomics studies in this powerful model organism." @default.
- W2944714048 created "2019-05-16" @default.
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- W2944714048 date "2019-01-01" @default.
- W2944714048 modified "2023-10-06" @default.
- W2944714048 title "Proximity-dependent biotinylation by TurboID to identify protein-protein interaction networks in yeast" @default.
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- W2944714048 doi "https://doi.org/10.1242/jcs.232249" @default.
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