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Annu Rev Genet. 2013 Jun 26. [Epub ahead of print]

Supramolecular Evolution of Protein Organization.

Author information

  • Instituto Argentino de Matemática "Alberto P. Calderón," CONICET (National Research Council), Buenos Aires 1083, Argentina and Collegium Basilea, Institute of Advanced Study, CH 4053, Basel, Switzerland; email: ariel@prowdsciences.com.


Protein associations, whether transient or long-lasting, determine cellular processes and enable the cooperative and regulated functionalities characteristic of complex organisms. From a broad physical perspective, soluble natural proteins represent a unique kind of solute prone to associate but not to precipitate. Thus, discrete reproducible associations define the protein supramolecular organization. The evolutionary forces that enable and promote this complexity are the subject matter of this review. The central problem addressed involves the paradoxical constructive role of random genetic drift, typically mildly deleterious, in fostering interactome complexity. By introducing biophysical insights in molecular evolution, we are able to identify the adaptive and nonadaptive elements that define the protein association propensity. We emphasize the mechanistic importance of population size and selection inefficiency in creating an evolutionary niche to promote interactome complexity. Finally, we describe the fitness catastrophes that result from the prevailing evolutionary strategy. Expected final online publication date for the Annual Review of Genetics Volume 47 is November 23, 2013. Please see http://www.annualreviews.org/catalog/pubdates.aspx for revised estimates.

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