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Proteome survey reveals modularity of the yeast cell machinery | | Anne-Claude Gavin
; Patrick Aloy
; Paola Grandi
; Rol
; 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 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
; | | Date: |
30 Mar 2006 | | Journal: | Nature, 440 (7084), 631-6 | | 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. | | Source: | PubMed, pmid16429126 doi: 10.1038/nature04532 | | Services: | Forum | Review | Favorites | |
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