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Comparative interactomics analysis of protein family interaction networks using PSIMAP (protein structural interactome map

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Lappe,  Michael
Independent Junior Research Groups (OWL), Max Planck Institute for Molecular Genetics, Max Planck Society;

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Park, D., Lee, S., Bolser, D., Schroeder, M., Lappe, M., Oh, D., et al. (2005). Comparative interactomics analysis of protein family interaction networks using PSIMAP (protein structural interactome map. Bioinformatics, 21(15), 3234-3240. doi:10.1093/bioinformatics/bti512.


Zitierlink: https://hdl.handle.net/11858/00-001M-0000-0010-8644-7
Zusammenfassung
Motivation: Many genomes have been completely sequenced. However, detecting and analyzing their protein–protein interactions by experimental methods such as co-immunoprecipitation, tandem affinity purification and Y2H is not as fast as genome sequencing. Therefore, a computational prediction method based on the known protein structural interactions will be useful to analyze large-scale protein–protein interaction rules within and among complete genomes. Results: We confirmed that all the predicted protein family interactomes (the full set of protein family interactions within a proteome) of 146 species are scale-free networks, and they share a small core network comprising 36 protein families related to indispensable cellular functions. We found two fundamental differences among prokaryotic and eukaryotic interactomes: (1) eukarya had significantly more hub families than archaea and bacteria and (2) certain special hub families determined the topology of the eukaryotic interactomes. Our comparative analysis suggests that a very small number of expansive protein families led to the evolution of interactomes and seemed to have played a key role in species diversification.