| STUDY |
Both groups use "bait" proteins to fish out protein interactions. Yeast proteins are turned into bait by attaching a tag that allows them to be captured in an immunoaffinity purification. The captured complexes are then separated by gel electrophoresis, and excised gel spots are analyzed by mass spectrometry (MS). A team of scientists from MDS Proteomics in Toronto and Odense, Denmark; Mount Sinai Hospital in Toronto; and the University of Toronto used the method to detect 3,617 protein interactions, starting with 725 bait proteins. The techniques in the Nature papers answer different questions than the yeast two-hybrid method, says Daniel Figeys, vice president of analytical sciences at MDS Proteomics. "The main question that yeast two-hybrid attempts to answer is: 'Is protein A binding to protein B?' Our approach answers the questions: 'What is the identity of all the proteins binding to protein A?' and 'What are the different complexes that protein A is involved in?' and 'What pathways is protein A involved in?' with no prior knowledge of the interacting partners of protein A," Figeys says. |
| UPDATE | 01.02 |
| AUTHOR |
- MDS Proteomics - Mount Sinai Hospital - Uni. Toronto |
| LITERATURE REF. | Nature, 415, p. 180 (2002) |
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