An evolutionary and structural characterization of mammalian protein complex organization

Autor: Matthias Oesterheld, Bernd Geissler, Philip Wong, Dmitrij Frishman, Andreas Kirschner, Andrea Hildebrand, Philipp Pagel, Andreas Ruepp, Thorsten Schmidt, Pawel Smialowski, Normann Strack, Florian Blöchl, Fabian J. Theis, Sonja Althammer
Rok vydání: 2008
Předmět:
Zdroj: BMC Genomics
BMC Genomics, Vol 9, Iss 1, p 629 (2008)
BMC Genomics 9:629 (2008)
ISSN: 1471-2164
Popis: 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 tends 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. Conclusion We observed similar trends in yeast and other data. Our results support the existence of conserved relations associated with the mammalian protein complexes.
Databáze: OpenAIRE
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