Experimental evolution of adenylate kinase reveals contrasting strategies toward protein thermostability.

ABSTRACT: Success in evolution depends critically upon the ability of organisms to adapt, a property that is also true for the proteins that contribute to the fitness of an organism. Successful protein evolution is enhanced by mutational pathways that generate a wide range of physicochemical mechanisms to adaptation. In an earlier study, we used a weak-link method to favor changes to an essential but maladapted protein, adenylate kinase (AK), within a microbial population. Six AK mutants (a single mutant followed by five double mutants) had success within the population, revealing a diverse range of adaptive strategies that included changes in nonpolar packing, protein folding dynamics, and formation of new hydrogen bonds and electrostatic networks. The first mutation, AK(BSUB) Q199R, was essential

SUBMITTER: Miller C 

PROVIDER: S-EPMC2913193 | biostudies-literature | 2010 Aug

REPOSITORIES: biostudies-literature