| Letter Bioinformatics Analysis of Experimentally Determined Protein Complexes in the Yeast (2009) | |||||||||||||||
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| Many important cellular functions are implemented by protein complexes that act as sophisticated molecular machines of varying size and temporal stability. Here we demonstrate quantitatively that protein complexes in the yeast Saccharomyces cerevisiae are comprised of a core in which subunits are highly coexpressed, display the same deletion phenotype (essential or nonessential), and share identical functional classification and cellular localization. This core is surrounded by a functionally mixed group of proteins, which likely represent short-lived or spurious attachments. The results allow us to define the deletion phenotype and cellular task of most known complexes, and to identify with high confidence the biochemical role of hundreds of proteins with yet unassigned functionality. [Supplemental material is available online at www.genome.org.] Large-scale mass-spectrometric studies in Saccharomyces cerevisiae provide a compendium of protein complexes (Alberts 1998; Hartwell et al. 1999) that are considered to play a key role in carrying out yeast functionality (Gavin et al. 2002; Ho et al. 2002). Althoughvastly informative, suchlibraries offer information only on the composition of a protein complex at a given time and developmental or environmental condition. In addition, | |||||||||||||||
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