Functional organization of the yeast proteome by systematic analysis of protein complexes

Anne-Claude Gavin (), Markus Bösche, Roland Krause, Paola Grandi, Martina Marzioch, Andreas Bauer, Jörg Schultz, Jens M. Rick, Anne-Marie Michon, Cristina-Maria Cruciat, Marita Remor, Christian Höfert, Malgorzata Schelder, Miro Brajenovic, Heinz Ruffner, Alejandro Merino, Karin Klein, Manuela Hudak, David Dickson, Tatjana Rudi, Volker Gnau, Angela Bauch, Sonja Bastuck, Bettina Huhse, Christina Leutwein, Marie-Anne Heurtier, Richard R. Copley, Angela Edelmann, Erich Querfurth, Vladimir Rybin, Gerard Drewes, Manfred Raida, Tewis Bouwmeester, Peer Bork, Bertrand Seraphin, Bernhard Kuster, Gitte Neubauer and Giulio Superti-Furga ()
Additional contact information
Anne-Claude Gavin: Cellzome AG
Markus Bösche: Cellzome AG
Roland Krause: Cellzome AG
Paola Grandi: Cellzome AG
Martina Marzioch: Cellzome AG
Andreas Bauer: Cellzome AG
Jörg Schultz: Cellzome AG
Jens M. Rick: Cellzome AG
Anne-Marie Michon: Cellzome AG
Cristina-Maria Cruciat: Cellzome AG
Marita Remor: Cellzome AG
Christian Höfert: Cellzome AG
Malgorzata Schelder: Cellzome AG
Miro Brajenovic: Cellzome AG
Heinz Ruffner: Cellzome AG
Alejandro Merino: Cellzome AG
Karin Klein: Cellzome AG
Manuela Hudak: Cellzome AG
David Dickson: Cellzome AG
Tatjana Rudi: Cellzome AG
Volker Gnau: Cellzome AG
Angela Bauch: Cellzome AG
Sonja Bastuck: Cellzome AG
Bettina Huhse: Cellzome AG
Christina Leutwein: Cellzome AG
Marie-Anne Heurtier: Cellzome AG
Richard R. Copley: European Molecular Biology Laboratory
Angela Edelmann: Cellzome AG
Erich Querfurth: Cellzome AG
Vladimir Rybin: Cellzome AG
Gerard Drewes: Cellzome AG
Manfred Raida: Cellzome AG
Tewis Bouwmeester: Cellzome AG
Peer Bork: European Molecular Biology Laboratory
Bertrand Seraphin: European Molecular Biology Laboratory
Bernhard Kuster: Cellzome AG
Gitte Neubauer: Cellzome AG
Giulio Superti-Furga: Cellzome AG

Nature, 2002, vol. 415, issue 6868, 141-147

Abstract: Abstract Most cellular processes are carried out by multiprotein complexes. The identification and analysis of their components provides insight into how the ensemble of expressed proteins (proteome) is organized into functional units. We used tandem-affinity purification (TAP) and mass spectrometry in a large-scale approach to characterize multiprotein complexes in Saccharomyces cerevisiae. We processed 1,739 genes, including 1,143 human orthologues of relevance to human biology, and purified 589 protein assemblies. Bioinformatic analysis of these assemblies defined 232 distinct multiprotein complexes and proposed new cellular roles for 344 proteins, including 231 proteins with no previous functional annotation. Comparison of yeast and human complexes showed that conservation across species extends from single proteins to their molecular environment. Our analysis provides an outline of the eukaryotic proteome as a network of protein complexes at a level of organization beyond binary interactions. This higher-order map contains fundamental biological information and offers the context for a more reasoned and informed approach to drug discovery.

Date: 2002
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DOI: 10.1038/415141a

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