Proteome survey reveals modularity of the yeast cell machinery

Research output: Contribution to journalJournal articleResearchpeer-review

  • Anne-Claude Gavin
  • Patrick Aloy
  • Paola Grandi
  • Roland Krause
  • Markus Boesche
  • Martina Marzioch
  • Christina Rau
  • Sonja Bastuck
  • Birgit Dümpelfeld
  • Angela Edelmann
  • Marie-Anne Heurtier
  • Verena Hoffman
  • Christian Hoefert
  • Karin Klein
  • Manuela Hudak
  • Anne-Marie Michon
  • Malgorzata Schelder
  • Markus Schirle
  • Marita Remor
  • Tatjana Rudi
  • Sean Hooper
  • Andreas Bauer
  • Tewis Bouwmeester
  • Georg Casari
  • Gerard Drewes
  • Gitte Neubauer
  • Jens M Rick
  • Bernhard Kuster
  • Peer Bork
  • Robert B Russell
  • Giulio Superti-Furga
Protein complexes are key molecular entities that integrate multiple gene products to perform cellular functions. Here we report the first genome-wide screen for complexes in an organism, budding yeast, using affinity purification and mass spectrometry. Through systematic tagging of open reading frames (ORFs), the majority of complexes were purified several times, suggesting screen saturation. The richness of the data set enabled a de novo characterization of the composition and organization of the cellular machinery. The ensemble of cellular proteins partitions into 491 complexes, of which 257 are novel, that differentially combine with additional attachment proteins or protein modules to enable a diversification of potential functions. Support for this modular organization of the proteome comes from integration with available data on expression, localization, function, evolutionary conservation, protein structure and binary interactions. This study provides the largest collection of physically determined eukaryotic cellular machines so far and a platform for biological data integration and modelling.
Original languageEnglish
JournalNature Study
Issue number7084
Pages (from-to)631-6
Number of pages6
Publication statusPublished - 2006
Externally publishedYes

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