Evolutionary trend toward kinetic stability in the folding trajectory of RNases H.

ABSTRACT: Proper folding of proteins is critical to producing the biological machinery essential for cellular function. The rates and energetics of a protein's folding process, which is described by its energy landscape, are encoded in the amino acid sequence. Over the course of evolution, this landscape must be maintained such that the protein folds and remains folded over a biologically relevant time scale. How exactly a protein's energy landscape is maintained or altered throughout evolution is unclear. To study how a protein's energy landscape changed over time, we characterized the folding trajectories of ancestral proteins of the ribonuclease H (RNase H) family using ancestral sequence reconstruction to access the evolutionary history between RNases H from mesophilic and thermophilic bacteria.

SUBMITTER: Lim SA 

PROVIDER: S-EPMC5135364 | biostudies-literature | 2016 Nov

REPOSITORIES: biostudies-literature