Pesquisa de proteoma revela a modularidade da maquinaria celular da levedura

Nature 440, 631-636 (30 March 2006) | doi:10.1038/nature04532; Received 17 October 2005; ; Accepted 15 December 2005

Proteome survey reveals modularity of the yeast cell machinery

Anne-Claude Gavin^1,6,5, Patrick Aloy^2,6, Paola Grandi¹, Roland Krause^1,3, Markus Boesche¹, Martina Marzioch¹, Christina Rau¹, Lars Juhl Jensen², Sonja Bastuck¹, Birgit Dümpelfeld¹, Angela Edelmann¹, Marie-Anne Heurtier¹, Verena Hoffman¹, Christian Hoefert¹, Karin Klein¹, Manuela Hudak¹, Anne-Marie Michon¹, Malgorzata Schelder¹, Markus Schirle¹, Marita Remor¹, Tatjana Rudi¹, Sean Hooper², Andreas Bauer¹, Tewis Bouwmeester¹, Georg Casari¹, Gerard Drewes¹, Gitte Neubauer¹, Jens M. Rick¹, Bernhard Kuster¹, Peer Bork², Robert B. Russell²and Giulio Superti-Furga^1,4

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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.

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1. Cellzome AG, Meyerhofstrasse 1, 69117 Heidelberg, Germany
2. EMBL, Meyerhofstrasse 1, 69117 Heidelberg, Germany
3. MPI-MG, MPI-IB, Charité Campus Mitte, Schumannstrasse 21/22, 10117 Berlin, Germany
4. Center for Molecular Medicine of the Austrian Academy of Sciences, Lazarettgasse 19, 1090 Vienna, Austria
5. †Present address: EMBL, Meyerhofstrasse 1, 69117 Heidelberg, Germany
6. *These authors contributed equally to this work

Correspondence to: Robert B. Russell²Giulio Superti-Furga^1,4 Correspondence and requests for materials should be addressed to G.S.-F. (Email: gsuperti@cemm.oeaw.ac.at), R.B.R. (Email: russell@embl-heidelberg.de). Purification and complex data have been deposited at the IntAct database with accession numbers EBI-768904 (purifications) and EBI-765905 (author inferred complexes). The data, including the MS protein identifications, are accessible athttp://yeast-complexes.embl.de, and the yeast strains are available from Euroscarf.

Received 17 October 2005 | Accepted 15 December 2005 |

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NOTA IMPERTINENTE DESTE BLOGGER:

Darwin também desconhecia totalmente tudo isso acima. É muita complexidade biológica do século 21 para o caminhãozinho de Darwin do século 19.


Gente, Darwin não explica isso. Kaput, teoria da evolução através da seleção natural!!!

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