Proteome survey reveals modularity of the yeast cell machinery
- PMID: 16429126
- DOI: 10.1038/nature04532
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.
Similar articles
-
Proteomics: where's Waldo in yeast?Nature. 2003 Oct 16;425(6959):671-2. doi: 10.1038/425671a. Nature. 2003. PMID: 14562083 No abstract available.
-
Analysis of the Saccharomyces cerevisiae proteome with PeptideAtlas.Genome Biol. 2006;7(11):R106. doi: 10.1186/gb-2006-7-11-r106. Genome Biol. 2006. PMID: 17101051 Free PMC article.
-
Playing tag with the yeast proteome.Nat Biotechnol. 2003 Nov;21(11):1297-9. doi: 10.1038/nbt1103-1297. Nat Biotechnol. 2003. PMID: 14595360 No abstract available.
-
Capturing cellular machines by systematic screens of protein complexes.Trends Microbiol. 2006 Aug;14(8):336-9. doi: 10.1016/j.tim.2006.06.002. Epub 2006 Jun 16. Trends Microbiol. 2006. PMID: 16782340 Review.
-
Mass-Spectrometry-Based Near-Complete Draft of the Saccharomyces cerevisiae Proteome.J Proteome Res. 2021 Feb 5;20(2):1328-1340. doi: 10.1021/acs.jproteome.0c00721. Epub 2021 Jan 14. J Proteome Res. 2021. PMID: 33443437 Review.
Cited by
-
Computational Approaches to Predict Protein-Protein Interactions in Crowded Cellular Environments.Chem Rev. 2024 Apr 10;124(7):3932-3977. doi: 10.1021/acs.chemrev.3c00550. Epub 2024 Mar 27. Chem Rev. 2024. PMID: 38535831 Free PMC article. Review.
-
Emerging Role of GCN1 in Disease and Homeostasis.Int J Mol Sci. 2024 Mar 5;25(5):2998. doi: 10.3390/ijms25052998. Int J Mol Sci. 2024. PMID: 38474243 Free PMC article. Review.
-
Evidence that Xrn1 is in complex with Gcn1, and is required for full levels of eIF2α phosphorylation.Biochem J. 2024 Apr 10;481(7):481-498. doi: 10.1042/BCJ20220531. Biochem J. 2024. PMID: 38440860 Free PMC article.
-
From beer to breadboards: yeast as a force for biological innovation.Genome Biol. 2024 Jan 4;25(1):10. doi: 10.1186/s13059-023-03156-9. Genome Biol. 2024. PMID: 38178179 Free PMC article. Review.
-
Single-cell imaging of protein dynamics of paralogs reveals mechanisms of gene retention.bioRxiv [Preprint]. 2023 Nov 23:2023.11.23.568466. doi: 10.1101/2023.11.23.568466. bioRxiv. 2023. PMID: 38045359 Free PMC article. Preprint.
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases