Comparing mutagenesis and simulations as tools for identifying functionally important sequence changes for protein thermal adaptation.

ABSTRACT: Comparative studies of orthologous proteins of species evolved at different temperatures have revealed consistent patterns of temperature-related variation in thermal stabilities of structure and function. However, the precise mechanisms by which interspecific variations in sequence foster these adaptive changes remain largely unknown. Here, we compare orthologs of cytosolic malate dehydrogenase (cMDH) from marine molluscs adapted to temperatures ranging from -1.9 °C (Antarctica) to ∼55 °C (South China coast) and show how amino acid usage in different regions of the enzyme (surface, intermediate depth, and protein core) varies with adaptation temperature. This eukaryotic enzyme follows some but not all of the rules established in comparisons of archaeal and bacterial proteins. To link the

SUBMITTER: Liao ML 

PROVIDER: S-EPMC6329985 | biostudies-literature | 2019 Jan

REPOSITORIES: biostudies-literature