Abstract
A protein interaction map for 12 of the 13 WW domains present in the proteins of S. cerevisiae was generated by using protein microarray data.
Highlights
The WW domain is found in a large number of eukaryotic proteins implicated in a variety of cellular processes
Protein-protein interactions on the microarrays were detected by the addition of fluorophoreconjugated streptavidin, and individual spots on the microarray were visualized by fluorescence scanning (Figure 3a)
We defined high-confidence interactions to be those in which four independent observations of the interaction were made
Summary
The WW domain is found in a large number of eukaryotic proteins implicated in a variety of cellular processes. Methods for building protein interaction networks The assembly of networks of interacting proteins and genes has provided a new perspective on the organization and regulation of cellular processes, allowing the superimposition and interpretation of a variety of types of functional information [1]. The methods are complementary: Y2H identifies binary protein-protein interactions whereas AP-MS establishes the members of co-purifying protein complexes Both methods will likely be required to accurately model local topologies within large networks [7], and they have been used to interconnect thousands of proteins. AP-MS approaches demand that the epitope tag not affect a protein's proper folding and inclusion within a complex Because of these technical drawbacks, protein interaction maps are both incomplete and contain interactions that are not biologically relevant
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