An evolutionary and structural characterization of mammalian protein complex organization.
BMC Genomics 9:629 (2008)
Background: We have recently released a comprehensive, manually curated database of mammalian protein complexes called CORUM. Combining CORUM with other resources, we assembled a dataset of over 2700 mammalian complexes. The availability of a rich information resource allows us to search for organizational properties concerning these complexes. Results: As the complexity of a protein complex in terms of the number of unique subunits increases, we observed that the number of such complexes and the mean non-synonymous to synonymous substitution ratio of associated genes tend to decrease. Similarly, as the number of different complexes a given protein participates in increases, the number of such proteins and the substitution ratio of the associated gene also tend to decrease. These observations provide evidence relating natural selection and the organization of mammalian complexes. We also observed greater homogeneity in terms of predicted protein isoelectric points, secondary structure and substitution ratio in annotated versus randomly generated complexes. A large proportion of the protein content and interactions in the complexes could be predicted from known binary protein-protein and domain-domain interactions. In particular, we found that large proteins interact preferentially with much smaller proteins. Conclusions: We observed similar trends in yeast and other data. Our results support the existence of conserved relations associated with the mammalian protein complexes.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Schlagwörter INTERACTION NETWORKS; FUNCTIONAL MODULARITY; INTERACTION DATABASE; SECONDARY STRUCTURE; SEQUENCE EVOLUTION; GENETIC-DISORDERS; SYNONYMOUS SITES; YEAST PROTEINS; PREDICTION; SELECTION
ISSN (print) / ISBN 1471-2164
Zeitschrift BMC Genomics
Quellenangaben Band: 9, Artikelnummer: 629
Verlag BioMed Central