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

Autor: Angela Bauch, Tatjana Rudi, Bettina Huhse, Heinz Ruffner, Bernhard Kuster, Giulio Superti-Furga, Markus Bösche, Volker Gnau, Richard R. Copley, Bertrand Séraphin, Christina Leutwein, David Dickson, Jörg Schultz, Angela Edelmann, Malgorzata Schelder, Karin Klein, Roland Krause, Vladimir Rybin, Tewis Bouwmeester, Erich Querfurth, Gitte Neubauer, Martina Marzioch, Sonja Bastuck, Miro Brajenovic, Manfred Raida, Marie-Anne Heurtier, Manuela Hudak, Christian Höfert, Jens Rick, Anne-Claude Gavin, Anne-Marie Michon, Marita Remor, Gerard Drewes, Andreas Bauer, Alejandro Merino, Paola Grandi, Peer Bork, Cristina-Maria Cruciat
Jazyk: angličtina
Rok vydání: 2002
Předmět:
Zdroj: Nature, Vol. 415, No 6868 (2002) pp. 141-147
ISSN: 0028-0836
Popis: 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.
Databáze: OpenAIRE