First-step mutations for adaptation at elevated temperature increase capsid stability in a virus.

ABSTRACT: The relationship between mutation, protein stability and protein function plays a central role in molecular evolution. Mutations tend to be destabilizing, including those that would confer novel functions such as host-switching or antibiotic resistance. Elevated temperature may play an important role in preadapting a protein for such novel functions by selecting for stabilizing mutations. In this study, we test the stability change conferred by single mutations that arise in a G4-like bacteriophage adapting to elevated temperature. The vast majority of these mutations map to interfaces between viral coat proteins, suggesting they affect protein-protein interactions. We assess their effects by estimating thermodynamic stability using molecular dynamic simulations and measuring kinetic stabi

SUBMITTER: Lee KH 

PROVIDER: S-EPMC3183071 | biostudies-literature | 2011

REPOSITORIES: biostudies-literature