Cold adaptation of tRNA nucleotidyltransferases: A tradeoff in activity, stability and fidelity.

ABSTRACT: Cold adaptation is an evolutionary process that has dramatic impact on enzymatic activity. Increased flexibility of the protein structure represents the main evolutionary strategy for efficient catalysis and reaction rates in the cold, but is achieved at the expense of structural stability. This results in a significant activity-stability tradeoff, as it was observed for several metabolic enzymes. In polymerases, however, not only reaction rates, but also fidelity plays an important role, as these enzymes have to synthesize copies of DNA and RNA as exact as possible. Here, we investigate the effects of cold adaptation on the highly accurate CCA-adding enzyme, an RNA polymerase that uses an internal amino acid motif within the flexible catalytic core as a template to synthesize the CCA trip

SUBMITTER: Ernst FGM 

PROVIDER: S-EPMC5785979 | biostudies-literature | 2018 Jan

REPOSITORIES: biostudies-literature