Proteome survey reveals modularity of the yeast cell machinery

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Proteome survey reveals modularity of the yeast cell machinery. / 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.

In: Nature Study, Vol. 440, No. 7084, 2006, p. 631-6.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Gavin, A-C, Aloy, P, Grandi, P, Krause, R, Boesche, M, Marzioch, M, Rau, C, Jensen, LJ, Bastuck, S, Dümpelfeld, B, Edelmann, A, Heurtier, M-A, Hoffman, V, Hoefert, C, Klein, K, Hudak, M, Michon, A-M, Schelder, M, Schirle, M, Remor, M, Rudi, T, Hooper, S, Bauer, A, Bouwmeester, T, Casari, G, Drewes, G, Neubauer, G, Rick, JM, Kuster, B, Bork, P, Russell, RB & Superti-Furga, G 2006, 'Proteome survey reveals modularity of the yeast cell machinery', Nature Study, vol. 440, no. 7084, pp. 631-6. https://doi.org/10.1038/nature04532

APA

Gavin, A-C., Aloy, P., Grandi, P., Krause, R., Boesche, M., Marzioch, M., Rau, C., Jensen, L. J., Bastuck, S., Dümpelfeld, B., Edelmann, A., Heurtier, M-A., Hoffman, V., Hoefert, C., Klein, K., Hudak, M., Michon, A-M., Schelder, M., Schirle, M., ... Superti-Furga, G. (2006). Proteome survey reveals modularity of the yeast cell machinery. Nature Study, 440(7084), 631-6. https://doi.org/10.1038/nature04532

Vancouver

Gavin A-C, Aloy P, Grandi P, Krause R, Boesche M, Marzioch M et al. Proteome survey reveals modularity of the yeast cell machinery. Nature Study. 2006;440(7084):631-6. https://doi.org/10.1038/nature04532

Author

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. / Proteome survey reveals modularity of the yeast cell machinery. In: Nature Study. 2006 ; Vol. 440, No. 7084. pp. 631-6.

Bibtex

@article{109ab60fc6914476b34cf0e58d92c2bd,
title = "Proteome survey reveals modularity of the yeast cell machinery",
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 = "Anne-Claude Gavin and Patrick Aloy and Paola Grandi and Roland Krause and Markus Boesche and Martina Marzioch and Christina Rau and Jensen, {Lars Juhl} and Sonja Bastuck and Birgit D{\"u}mpelfeld and Angela Edelmann and Marie-Anne Heurtier and Verena Hoffman and Christian Hoefert and Karin Klein and Manuela Hudak and Anne-Marie Michon and Malgorzata Schelder and Markus Schirle and Marita Remor and Tatjana Rudi and Sean Hooper and Andreas Bauer and Tewis Bouwmeester and Georg Casari and Gerard Drewes and Gitte Neubauer and Rick, {Jens M} and Bernhard Kuster and Peer Bork and Russell, {Robert B} and Giulio Superti-Furga",
year = "2006",
doi = "10.1038/nature04532",
language = "English",
volume = "440",
pages = "631--6",
journal = "Nature Study",
issn = "0028-0860",
number = "7084",

}

RIS

TY - JOUR

T1 - Proteome survey reveals modularity of the yeast cell machinery

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 Juhl

AU - Bastuck, Sonja

AU - Dümpelfeld, 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 M

AU - Kuster, Bernhard

AU - Bork, Peer

AU - Russell, Robert B

AU - Superti-Furga, Giulio

PY - 2006

Y1 - 2006

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.

AB - 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.

U2 - 10.1038/nature04532

DO - 10.1038/nature04532

M3 - Journal article

C2 - 16429126

VL - 440

SP - 631

EP - 636

JO - Nature Study

JF - Nature Study

SN - 0028-0860

IS - 7084

ER -

ID: 40740453