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Legrain's group describes their strategy for mapping all protein-protein interactions in S. cerevisiae. A genomic library was screened with DNA-binding domain fusions of a small set of related proteins involved in RNA processing. Positives from the first screens that encode probable in vivo interactors are then used as baits in a second round of screens.
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This paper describes a membrane-associated two-hybrid system in yeast. Interacting protein fusions recruit Sos to the membrane where it stimulates guanyl nucleotide exchange on yeast Ras, rescuing a temperature-sensitive (Ras) mutant. The system was advanced as an alternative for study of proteins interacting with transcriptional activators, but should be particularly useful for membrane-associated proteins, which are often problematic for the original two-hybrid system.
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