Pleiotropic Tensegrity

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Science  01 Sep 2006:
Vol. 313, Issue 5791, pp. 1203
DOI: 10.1126/science.313.5791.1203b

Systems biology has popularized the view of metabolic and regulatory pathways as networks, and experimental and bioinformatics studies of protein-protein interactions have codified these networks as centralized hubs and radiating spokes. One somewhat deceptive implication inherent in these representations is the static character of these linkages.

Knight et al. provide a comprehensive proteomic analysis of Pseudomonas fluorescens SBW25, where spontaneous adaptive mutations in the wspF gene result in the ability to grow at the air/liquid interface (as opposed to within broth). Although the genetic difference between the parental SM (smooth morphology) and evolved LSWS (Large Spreading Wrinkly Spreader) strains corresponds to the replacement of a serine with an arginine in a single component of the Wsp chemotaxis pathway, there are significant differences in the amounts of 46 proteins (identified by mass spectrometry and recourse to the draft genome), primarily with functions in amino acid uptake and catabolism. Mapping the variation in the amounts of these proteins across independent replicate cultures revealed that the LSWS strain, in comparison to the original SM strain, exhibits a distinct network of covariation. These distributed, yet coordinated, changes in protein levels suggest that understanding network dynamics will be key to explaining pleiotropy. — GJC

Nat. Genet. 38, 10.1038/ng1867 (2006).

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