Interplay between chaperones and protein disorder promotes the evolution of protein networks.

ABSTRACT: Evolution is driven by mutations, which lead to new protein functions but come at a cost to protein stability. Non-conservative substitutions are of interest in this regard because they may most profoundly affect both function and stability. Accordingly, organisms must balance the benefit of accepting advantageous substitutions with the possible cost of deleterious effects on protein folding and stability. We here examine factors that systematically promote non-conservative mutations at the proteome level. Intrinsically disordered regions in proteins play pivotal roles in protein interactions, but many questions regarding their evolution remain unanswered. Similarly, whether and how molecular chaperones, which have been shown to buffer destabilizing mutations in individual proteins, genera

SUBMITTER: Pechmann S 

PROVIDER: S-EPMC4072544 | biostudies-literature | 2014 Jun

REPOSITORIES: biostudies-literature