IAM   02674
INSTITUTO ARGENTINO DE MATEMATICA ALBERTO CALDERON
Unidad Ejecutora - UE
artículos
Título:
Supramolecular evolution of protein organization
Autor/es:
ARIEL FERNANDEZ
Revista:
ANNUAL REVIEW OF GENETICS
Editorial:
ANNUAL REVIEWS
Referencias:
Lugar: Palo Alto, California; Año: 2013 vol. 47 p. 1 - 1
ISSN:
0066-4197
Resumen:
Abstract. 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 supra-molecular 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 identify the adaptive and non-adaptive 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.