An in Vivo Map of the Yeast Protein Interactome
Kirill Tarassov,1*
Vincent Messier,1*
Christian R. Landry,1,2*
Stevo Radinovic,1*
Mercedes M. Serna Molina,1
Igor Shames,1
Yelena Malitskaya,1
Jackie Vogel,3
Howard Bussey,3
Stephen W. Michnick1,2
Protein interactions regulate the systems-level behavior of cells; thus, deciphering the structure and dynamics of protein interaction networks in their cellular context is a central goal in biology. We have performed a genome-wide in vivo screen for protein-protein interactions in Saccharomyces cerevisiae by means of a protein-fragment complementation assay (PCA). We identified 2770 interactions among 1124 endogenously expressed proteins. Comparison with previous studies confirmed known interactions, but most were not known, revealing a previously unexplored subspace of the yeast protein interactome. The PCA detected structural and topological relationships between proteins, providing an 8-nanometer–resolution map of dynamically interacting complexes in vivo and extended networks that provide insights into fundamental cellular processes, including cell polarization and autophagy, pathways that are evolutionarily conserved and central to both development and human health.
1 Département de Biochimie, Université de Montréal Casier postal 6128, Succursale Centre-ville, Montréal, Québec H3C 3J7, Canada.
2 Centre Robert-Cedergren, Bio-Informatique et Génomique, Université de Montréal, C.P. 6128, Succursale Centre-ville, Montréal, Québec H3C 3J7, Canada.
3 Department of Biology, McGill University, 1205 Avenue Dr. Penfield, Montréal, Québec H3A 1B1, Canada.
* These authors contributed equally to this work.
To whom correspondence should be addressed. E-mail: stephen.michnick{at}umontreal.ca
