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An in vivo map of the yeast protein interactome.

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.

Pubmed ID: 18467557

Authors

  • Tarassov K
  • Messier V
  • Landry CR
  • Radinovic S
  • Serna Molina MM
  • Shames I
  • Malitskaya Y
  • Vogel J
  • Bussey H
  • Michnick SW

Journal

Science (New York, N.Y.)

Publication Data

June 13, 2008

Associated Grants

None

Mesh Terms

  • Autophagy
  • Cell Cycle
  • Cell Polarity
  • Genome, Fungal
  • Metabolic Networks and Pathways
  • Organelles
  • Protein Binding
  • Protein Folding
  • Protein Interaction Domains and Motifs
  • Protein Interaction Mapping
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Tetrahydrofolate Dehydrogenase