Split-BioID a conditional proteomics approach to monitor the composition of spatiotemporally defined protein complexes

Isabel Myriam Schopp, Cinthia Claudia Amaya Ramirez, Jerneja Debeljak, Elisa Kreibich, Merle Skribbe, Klemens Wild and Julien Béthune ()
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Isabel Myriam Schopp: CellNetworks Junior Research Group Posttranscriptional Regulation of mRNA Expression and Localization, Heidelberg University
Cinthia Claudia Amaya Ramirez: CellNetworks Junior Research Group Posttranscriptional Regulation of mRNA Expression and Localization, Heidelberg University
Jerneja Debeljak: CellNetworks Junior Research Group Posttranscriptional Regulation of mRNA Expression and Localization, Heidelberg University
Elisa Kreibich: CellNetworks Junior Research Group Posttranscriptional Regulation of mRNA Expression and Localization, Heidelberg University
Merle Skribbe: CellNetworks Junior Research Group Posttranscriptional Regulation of mRNA Expression and Localization, Heidelberg University
Klemens Wild: Biochemie-Zentrum Heidelberg (BZH)
Julien Béthune: CellNetworks Junior Research Group Posttranscriptional Regulation of mRNA Expression and Localization, Heidelberg University

Nature Communications, 2017, vol. 8, issue 1, 1-14

Abstract: Abstract Understanding the function of the thousands of cellular proteins is a central question in molecular cell biology. As proteins are typically part of multiple dynamic and often overlapping macromolecular complexes exerting distinct functions, the identification of protein–protein interactions (PPI) and their assignment to specific complexes is a crucial but challenging task. We present a protein fragments complementation assay integrated with the proximity-dependent biotinylation technique BioID. Activated on the interaction of two proteins, split-BioID is a conditional proteomics approach that allows in a single and simple assay to both experimentally validate binary PPI and to unbiasedly identify additional interacting factors. Applying our method to the miRNA-mediated silencing pathway, we can probe the proteomes of two distinct functional complexes containing the Ago2 protein and uncover the protein GIGYF2 as a regulator of miRNA-mediated translation repression. Hence, we provide a novel tool to study dynamic spatiotemporally defined protein complexes in their native cellular environment.

Date: 2017
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DOI: 10.1038/ncomms15690

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