Reference: Collins SR, et al. (2007) Toward a Comprehensive Atlas of the Physical Interactome of Saccharomyces cerevisiae. Mol Cell Proteomics 6(3):439-50

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Abstract

Defining protein complexes is critical to virtually all aspects of cell biology. Two recent affinity purification/mass spectrometry studies in Saccharomyces cerevisiae have vastly increased the available protein interaction data. The practical utility of such high-throughput interaction sets, however, is substantially decreased by the presence of false positives. Here we create a novel probabilistic metric that takes advantage of the high density of these data, including both the presence and absence of individual associations, to provide a measure of the relative confidence of each potential protein-protein interaction. This analysis largely overcomes the noise inherent in high-throughput immunoprecipitation experiments. For example, of the 12,122 binary interactions in the general repository of interaction data (BioGRID) derived from these two studies, we mark 7,504 as being of substantially lower confidence. Additionally, applying our metric and a stringent cutoff identifies a set of 9,074 interactions (including 4,456 which were not among the 12,122 interactions) with accuracy comparable to that of conventional small-scale methodologies. Finally, we organize proteins into coherent multi-subunit complexes using hierarchical clustering. This work thus provides a highly accurate physical interaction map of yeast in a format that is readily accessible to the biological community.

Reference Type
Journal Article
Authors
Collins SR, Kemmeren P, Zhao XC, Greenblatt JF, Spencer F, Holstege FC, Weissman JS, Krogan NJ
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Interaction Annotations

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Interactor Interactor Type Assay Annotation Action Modification Phenotype Source Reference

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