title: Exploiting amino acid composition for predicting protein-protein interactions.
abstract: BACKGROUND
  Computational prediction of protein interactions typically use protein domains as classifier features because they capture conserved information of interaction surfaces. However, approaches relying on domains as features cannot be applied to proteins without any domain information. In this paper, we explore the contribution of pure amino acid composition (AAC) for protein interaction prediction. This simple feature, which is based on normalized counts of single or pairs of amino acids, is applicable to proteins from any sequenced organism and can be used to compensate for the lack of domain information.
  
  
  RESULTS
  AAC performed at par with protein interaction prediction based on domains on three yeast protein interaction datasets. Similar behavior was obtained using different classifiers, indicating that our results are a function of features and not of classifiers. In addition to yeast datasets, AAC performed comparably on worm and fly datasets. Prediction of interactions for the entire yeast proteome identified a large number of novel interactions, the majority of which co-localized or participated in the same processes. Our high confidence interaction network included both well-studied and uncharacterized proteins. Proteins with known function were involved in actin assembly and cell budding. Uncharacterized proteins interacted with proteins involved in reproduction and cell budding, thus providing putative biological roles for the uncharacterized proteins.
  
  
  CONCLUSIONS
  AAC is a simple, yet powerful feature for predicting protein interactions, and can be used alone or in conjunction with protein domains to predict new and validate existing interactions. More importantly, AAC alone performs at par with existing, but more complex, features indicating the presence of sequence-level information that is predictive of interaction, but which is not necessarily restricted to domains.
authors: Sushmita Roy Computer Science, University of New Mexico, Albuquerque, New Mexico, United States of America. sroy@cs.unm.edu
authors: Sushmita
authors: S
authors: Roy
authors: Diego
authors: D
authors: Martinez
authors: Harriett
authors: H
authors: Platero
authors: Terran
authors: T
authors: Lane
authors: Margaret
authors: M
authors: Werner-Washburne
mesh_terms: D000465:Algorithms; D000596:Amino Acids / Q000737:chemistry*; D000818:Animals; D017173:Caenorhabditis elegans; D019295:Computational Biology / Q000379:methods; D019281:Dimerization; D004330:Drosophila; D019143:Evolution, Molecular; D005656:Fungal Proteins / Q000737:chemistry; D016366:Open Reading Frames; D011336:Probability; D025941:Protein Interaction Mapping; D011506:Proteins / Q000737:chemistry; D020543:Proteome; D040901:Proteomics / Q000379:methods
chemical_list: D000596:Amino Acids; D005656:Fungal Proteins; D011506:Proteins; D020543:Proteome