Dynamic structure mediates halophilic adaptation of a DNA polymerase from the deep‐sea brines of the Red Sea

What is it about?

The deep-sea brines of the Red Sea are remote and unexplored environments characterized by high temperatures, anoxic water and elevated concentrations of salt and heavy metals. This environment provides a rare system to study the interplay between halophilic and thermophilic adaptation in biological macromolecules. Here, we report the first DNA polymerase with halophilic and thermophilic features. By using structural analysis and enzymatic activity assays, we illustrate the first potential mechanisms of how an enzyme adapts to the opposing structural requirements of high salt concentration and temperature. Our knowledge provides a new engineering strategy for an enzyme to adapt to thermophilic and halophilic conditions.

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