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Evolutionary conservation of motif constituents in the yeast protein interaction network

Abstract

Understanding why some cellular components are conserved across species but others evolve rapidly is a key question of modern biology1,2,3. Here we show that in Saccharomyces cerevisiae, proteins organized in cohesive patterns of interactions are conserved to a substantially higher degree than those that do not participate in such motifs. We find that the conservation of proteins in distinct topological motifs correlates with the interconnectedness and function of that motif and also depends on the structure of the overall interactome topology. These findings indicate that motifs may represent evolutionary conserved topological units of cellular networks molded in accordance with the specific biological function in which they participate.

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Figure 1: Relationship between the topology of a protein interaction network and the evolutionary conservation of individual proteins.

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Acknowledgements

Research at the University of Notre Dame and Northwestern University was supported by grants from the US National Institutes of Health (National Institute of General Medical Sciences) and the Department of Energy Genomes to Life Program. Research at the University of Notre Dame was also supported by the National Science Foundation.

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Correspondence to Z N Oltvai or A-L Barabási.

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Wuchty, S., Oltvai, Z. & Barabási, AL. Evolutionary conservation of motif constituents in the yeast protein interaction network. Nat Genet 35, 176–179 (2003). https://doi.org/10.1038/ng1242

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