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Protein complexes in Saccharomyces cerevisiae |
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Author(s):
Gary Bader, Christopher Hogue |
Institution:
Samuel Lunenfeld Research Institute, Toronto |
Year:
2002 |
URL:
http://tinyurl.com/mbxkj |
Project Description:
The recent abundance of genome sequence data has brought an urgent need for systematic proteomics to decipher the encoded protein networks that dictate cellular function. To date, generation of large-scale protein?protein interaction maps has relied on the yeast two-hybrid system, which detects binary interactions through activation of reporter gene expression. With the advent of ultrasensitive mass spectrometric protein identification methods, it is feasible to identify directly protein complexes on a proteome-wide scale. In this paper, published in Nature magazine, the authors report, using the budding yeast Saccharomyces cerevisiae as a test case, an example of this approach, which they term high-throughput mass spectrometric protein complex identification (HMS-PCI). Beginning with 10% of predicted yeast proteins as baits, they detected 3,617 associated proteins covering 25% of the yeast proteome. Numerous protein complexes were identified, including many new interactions in various signaling pathways and in the DNA damage response.
The graph shown here, drawn with Pajek software, proves that the connectivity distribution of the HMS-PCI data set follows a power law, as observed for other large-scale biological networks.
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