Reverse gyrase is a DNA topoisomerase that is peculiar in many aspects: it has the unique ability to introduce positive supercoils into DNA molecules; it comprises a type IA topoisomerase fused to a helicase-like domain; although it is a type IA topoisomerase, its reaction is ATP-dependent; and it is the only hyperthermophile-specific protein. All these features have made reverse gyrase the subject of biochemical, structural and functional studies, although they have not shed complete light on the evolution, mechanism and function of this distinctive enzyme. In the present article, we review the latest progress on structure-function relationships of reverse gyrase, and discuss old and recent data linking reverse gyrase to DNA stability, protection and repair in hyperthermophilic organisms.
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