Proteome survey reveals modularity of the yeast cell machinery Export

@article{citeulike:477450, 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.}, author = {Gavin, Anne-Claude and Aloy, Patrick and Grandi, Paola and Krause, Roland and Boesche, Markus and Marzioch, Martina and Rau, Christina and Jensen, Lars J. and Bastuck, Sonja and Dumpelfeld, Birgit and Edelmann, Angela and Heurtier, Marie-Anne and Hoffman, Verena and Hoefert, Christian and Klein, Karin and Hudak, Manuela and Michon, Anne-Marie and Schelder, Malgorzata and Schirle, Markus and Remor, Marita and Rudi, Tatjana and Hooper, Sean and Bauer, Andreas and Bouwmeester, Tewis and Casari, Georg and Drewes, Gerard and Neubauer, Gitte and Rick, Jens M. and Kuster, Bernhard and Bork, Peer and Russell, Robert B. and Superti-Furga, Giulio}, citeulike-article-id = {477450}, citeulike-linkout-0 = {http://dx.doi.org/10.1038/nature04532}, citeulike-linkout-1 = {http://dx.doi.org/10.1038/nature04532}, citeulike-linkout-2 = {http://view.ncbi.nlm.nih.gov/pubmed/16429126}, citeulike-linkout-3 = {http://www.hubmed.org/display.cgi?uids=16429126}, day = {22}, doi = {10.1038/nature04532}, issn = {0028-0836}, journal = {Nature}, keywords = {bio-informatics, cell, complexes, high-throughput, large-scale, machinery, modularity, protein, proteome, proteomics, yeast}, month = {January}, number = {7084}, pages = {631--636}, posted-at = {2006-01-30 19:41:37}, priority = {4}, publisher = {Nature Publishing Group}, title = {Proteome survey reveals modularity of the yeast cell machinery}, url = {http://dx.doi.org/10.1038/nature04532}, volume = {440}, year = {2006} }

TY - JOUR ID - citeulike:477450 L3 - citeulike-article-id:477450 N2 - 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. IS - 7084 JF - Nature SN - 0028-0836 EP - 636 TI - Proteome survey reveals modularity of the yeast cell machinery PB - Nature Publishing Group VL - 440 SP - 631 KW - bio-informatics KW - cell KW - complexes KW - high-throughput KW - large-scale KW - machinery KW - modularity KW - protein KW - proteome KW - proteomics KW - yeast AU - Gavin, Anne-Claude AU - Aloy, Patrick AU - Grandi, Paola AU - Krause, Roland AU - Boesche, Markus AU - Marzioch, Martina AU - Rau, Christina AU - Jensen, Lars AU - Bastuck, Sonja AU - Dumpelfeld, Birgit AU - Edelmann, Angela AU - Heurtier, Marie-Anne AU - Hoffman, Verena AU - Hoefert, Christian AU - Klein, Karin AU - Hudak, Manuela AU - Michon, Anne-Marie AU - Schelder, Malgorzata AU - Schirle, Markus AU - Remor, Marita AU - Rudi, Tatjana AU - Hooper, Sean AU - Bauer, Andreas AU - Bouwmeester, Tewis AU - Casari, Georg AU - Drewes, Gerard AU - Neubauer, Gitte AU - Rick, Jens AU - Kuster, Bernhard AU - Bork, Peer AU - Russell, Robert AU - Superti-Furga, Giulio PY - 2006/01/22/ UR - http://dx.doi.org/10.1038/nature04532 ER -