Functional and topological characterization of protein interaction networks.

The elucidation of the cell's large-scale organization is a primary challenge for post-genomic biology, and understanding the structure of protein interaction networks offers an important starting point for such studies. We compare four available databases that approximate the protein interaction network of the yeast, Saccharomyces cerevisiae, aiming to uncover the network's generic large-scale properties and the impact of the proteins' function and cellular localization on the network topology. We show how each database supports a scale-free, topology with hierarchical modularity, indicating that these features represent a robust and generic property of the protein interactions network. We also find strong correlations between the network's structure and the functional role and subcellular localization of its protein constituents, concluding that most functional and/or localization classes appear as relatively segregated subnetworks of the full protein interaction network. The uncovered systematic differences between the four protein interaction databases reflect their relative coverage for different functional and localization classes and provide a guide for their utility in various bioinformatics studies.