Sign on

SAO/NASA ADS General Science Abstract Service

· Find Similar Abstracts (with default settings below)
· Electronic Refereed Journal Article (HTML)
· References in the article
· Citations to the Article (27) (Citation History)
· Refereed Citations to the Article
· Also-Read Articles (Reads History)
·
· Translate This Page
Title:
Proteome survey reveals modularity of the yeast cell machinery
Authors:
Gavin, Anne-Claude; Aloy, Patrick; Grandi, Paola; Krause, Roland; Boesche, Markus; Marzioch, Martina; Rau, Christina; Jensen, Lars Juhl; Bastuck, Sonja; Dümpelfeld, Birgit; Edelmann, Angela; Heurtier, Marie-Anne; Hoffman, Verena; Hoefert, Christian; Klein, Karin; Hudak, Manuela; Michon, Anne-Marie; Schelder, Malgorzata; Schirle, Markus; Remor, Marita; Rudi, Tatjana; Hooper, Sean; Bauer, Andreas; Bouwmeester, Tewis; Casari, Georg; Drewes, Gerard; Neubauer, Gitte; Rick, Jens M.; Kuster, Bernhard; Bork, Peer; Russell, Robert B.; Superti-Furga, Giulio
Affiliation:
AA(Cellzome AG, Meyerhofstrasse 1, 69117 Heidelberg, Germany), AB(EMBL, Meyerhofstrasse 1, 69117 Heidelberg, Germany), AC(Cellzome AG, Meyerhofstrasse 1, 69117 Heidelberg, Germany), AD(Cellzome AG, Meyerhofstrasse 1, 69117 Heidelberg, Germany), AE(Cellzome AG, Meyerhofstrasse 1, 69117 Heidelberg, Germany), AF(Cellzome AG, Meyerhofstrasse 1, 69117 Heidelberg, Germany), AG(Cellzome AG, Meyerhofstrasse 1, 69117 Heidelberg, Germany), AH(EMBL, Meyerhofstrasse 1, 69117 Heidelberg, Germany), AI(Cellzome AG, Meyerhofstrasse 1, 69117 Heidelberg, Germany), AJ(Cellzome AG, Meyerhofstrasse 1, 69117 Heidelberg, Germany), AK(Cellzome AG, Meyerhofstrasse 1, 69117 Heidelberg, Germany), AL(Cellzome AG, Meyerhofstrasse 1, 69117 Heidelberg, Germany), AM(Cellzome AG, Meyerhofstrasse 1, 69117 Heidelberg, Germany), AN(Cellzome AG, Meyerhofstrasse 1, 69117 Heidelberg, Germany), AO(Cellzome AG, Meyerhofstrasse 1, 69117 Heidelberg, Germany), AP(Cellzome AG, Meyerhofstrasse 1, 69117 Heidelberg, Germany), AQ(Cellzome AG, Meyerhofstrasse 1, 69117 Heidelberg, Germany), AR(Cellzome AG, Meyerhofstrasse 1, 69117 Heidelberg, Germany), AS(Cellzome AG, Meyerhofstrasse 1, 69117 Heidelberg, Germany), AT(Cellzome AG, Meyerhofstrasse 1, 69117 Heidelberg, Germany), AU(Cellzome AG, Meyerhofstrasse 1, 69117 Heidelberg, Germany), AV(EMBL, Meyerhofstrasse 1, 69117 Heidelberg, Germany), AW(Cellzome AG, Meyerhofstrasse 1, 69117 Heidelberg, Germany), AX(Cellzome AG, Meyerhofstrasse 1, 69117 Heidelberg, Germany), AY(Cellzome AG, Meyerhofstrasse 1, 69117 Heidelberg, Germany), AZ(Cellzome AG, Meyerhofstrasse 1, 69117 Heidelberg, Germany), BA(Cellzome AG, Meyerhofstrasse 1, 69117 Heidelberg, Germany), BB(Cellzome AG, Meyerhofstrasse 1, 69117 Heidelberg, Germany), BC(Cellzome AG, Meyerhofstrasse 1, 69117 Heidelberg, Germany), BD(EMBL, Meyerhofstrasse 1, 69117 Heidelberg, Germany), BE(EMBL, Meyerhofstrasse 1, 69117 Heidelberg, Germany), BF(Cellzome AG, Meyerhofstrasse 1, 69117 Heidelberg, Germany)
Publication:
Nature, Volume 440, Issue 7084, pp. 631-636 (2006). (Nature Homepage)
Publication Date:
03/2006
Origin:
NATURE
Abstract Copyright:
(c) 2006: Nature
DOI:
10.1038/nature04532
Bibliographic Code:
2006Natur.440..631G

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.
Bibtex entry for this abstract   Preferred format for this abstract (see Preferences)
   

Find Similar Abstracts:

Use: Authors
Title
Abstract Text
Return: Query Results Return    items starting with number
Query Form
Database: Astronomy
Physics
arXiv e-prints