title: Reverse gyrase and genome stability in hyperthermophilic organisms.
abstract: 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.
authors.affiliation: Institute of Protein Biochemistry, Consiglio Nazionale delle Ricerche, Via P. Castellino 111, 80131 Naples, Italy.
authors.forename: Giuseppe
authors.initials: G
authors.lastname: Perugino
authors.forename: Anna
authors.initials: A
authors.lastname: Valenti
authors.forename: Anna
authors.initials: A
authors.lastname: D'amaro
authors.forename: Mosè
authors.initials: M
authors.lastname: Rossi
authors.forename: Maria
authors.initials: M
authors.lastname: Ciaramella
mesh_terms: D001105:Archaea / Q000201:enzymology* / Q000235:genetics*; D004260:DNA Repair; D004264:DNA Topoisomerases, Type I / Q000737:chemistry / Q000378:metabolism*; D042822:Genomic Instability; D017434:Protein Structure, Tertiary; D013045:Species Specificity
chemical_list: C041813:DNA reverse gyrase; D004264:DNA Topoisomerases, Type I