Proteome survey reveals modularity of the yeast cell machinery

Anne Claude Gavin, Patrick Aloy, Paola Grandi, Roland Krause, Markus Boesche, Martina Marzioch, Christina Rau, Lars Juhl Jensen, 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 RemorTatjana 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

Research output: Contribution to journalArticlepeer-review

2176 Scopus citations

Abstract

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
Pages (from-to)631-636
Number of pages6
JournalNature
Volume440
Issue number7084
DOIs
StatePublished - 30 Mar 2006
Externally publishedYes

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