Catalysis of protein folding by chaperones accelerates evolutionary dynamics in adapting cell populations.

ABSTRACT: Although molecular chaperones are essential components of protein homeostatic machinery, their mechanism of action and impact on adaptation and evolutionary dynamics remain controversial. Here we developed a physics-based ab initio multi-scale model of a living cell for population dynamics simulations to elucidate the effect of chaperones on adaptive evolution. The 6-loci genomes of model cells encode model proteins, whose folding and interactions in cellular milieu can be evaluated exactly from their genome sequences. A genotype-phenotype relationship that is based on a simple yet non-trivially postulated protein-protein interaction (PPI) network determines the cell division rate. Model proteins can exist in native and molten globule states and participate in functional and all possible p

SUBMITTER: Cetinbas M 

PROVIDER: S-EPMC3820506 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature