Abstract
Scale-free networks have become a topic of intense interest because of the potential to develop theories universally applicable to networks representing social interactions, internet connectivity, and biological processes. Scale-free topology is associated with power-law distributions of connectivity, in which most network components have only few connections while a very few components are extremely highly-connected. Here we investigate the power-law and scale-free properties of the network corresponding to protein-protein interactions in Drosophila melanogaster. We examine power-law behavior with a standard statistical technique designed to distinguish whether a power-law fit is adequate to describe the vertex degree distribution. We find that the degree distribution for the entire network, consisting of baits and preys, decays faster than power law. This fit may be confounded by artifacts of the screening procedure. The prey-only degree distribution is less likely to be confounded by the screening procedure, and is fit adequately by a power-law. When only the biologically relevant interactions are considered, however, the degree distribution again decays faster than power-law. Thus, power-law behavior may reflect interactions that are observed in vitro but not in vivo. We next describe an algorithm that may be able to extract the true distribution from the incomplete data. Finally, we investigate scale-free properties by characterizing organizational patterns over increasing spatial scales. We provide evidence for the existence of a length-scale that characterizes organization in the network. The existence of such a correlation length stands in contrast to scale-free networks, in which no length scale is special. These results suggest that the Drosophila protein interaction network may not be power-law and is not scale-free.
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References
Giot L, Bader JS, Brouwer C et al. A protein interaction map of Drosophila melanogaster. Science 2003; 302:1727–1736.
Uetz P, Giot L, Cagney G et al. A comprehensive analysis of protein-protein interactions in Saccharomyces cerevisiae. Nature 2000; 403:623–627.
Ito T, Chiba T, Ozawa R et al. A comprehensive two-hybrid analysis to explore the yeast protein interactome. Proc Natl Acad Sci USA 2001; 98:4569–4574.
Gavin AC, Bosche M, Krause R et al. Functional organization of the yeast proteome by systematic analysis of protein complexes. Nature 2002; 415:141–147.
Ho Y, Gruhler A, Heilbut A et al. Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry. Nature 2002; 415:180–183.
Lee TI, Rinaldi NJ, Robert F et al. Transcriptional regulatory networks in Saccharomyces cerevisiae. Science 2002; 298:799–804.
Watts DJ, Strogatz SH. Collective dynamics of’ small-world’ networks. Nature 1998; 393:440–442.
Barabasi AL, Albert R. Emergence of scaling in random networks. Science 1999; 286:509–512.
von Mering C et al. Comparative assessment of large-scale data sets of protein-protein interactions. Nature 2002; 417:399–403.
Deane CM, Salwinski L, Xenarios I et al. Protein interactions: two methods for assessment of the reliability of high throughput observations. Mol Cell Proteomics 2002; 1:349–356.
Bader JS, Chaudhuri A, Rothberg JM et al. Gaining confidence in high-throughput protein interaction networks. Nat Biotechnol 2004; 22:00–00.
Mossa S, Barthelemy M, Eugene Stanley H et al. Truncation of power law behavior in “scale-free” network models due to information filtering. Phys Rev Lett 2002; 88:138701.
Goldberg DS, Roth FP. Assessing experimentally derived interactions in a small world. Proc Natl Acad Sci USA 2003; 100:4372–4376.
Ravasz E, Somera AL, Mongru DA et al. Hierarchical organization of modularity in metabolic networks. Science 2002; 297:1551–1555.
Jin EM, Girvan M, Newman ME. Structure of growing social networks. Phys Rev E Stat Nonlin Soft Matter Phys 2001; 64:046132.
Carlson JM, Doyle J. Complexity and robustness. Proc Natl Acad Sci USA 2002; 99(Suppl 1):2538–2545.
Newman ME, Girvan M, Farmer JD. Optimal design, robustness, and risk aversion. Phys Rev Lett 2002; 89:028301.
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Bader, J.S. (2006). The Drosophila Protein Interaction Network May Be neither Power-Law nor Scale-Free. In: Power Laws, Scale-Free Networks and Genome Biology. Molecular Biology Intelligence Unit. Springer, Boston, MA. https://doi.org/10.1007/0-387-33916-7_5
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DOI: https://doi.org/10.1007/0-387-33916-7_5
Publisher Name: Springer, Boston, MA
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