Reverse gyrase and genome stability in hyperthermophilic organisms.
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.
Perugino
Giuseppe
G
Institute of Protein Biochemistry, Consiglio Nazionale delle Ricerche, Via P. Castellino 111, 80131 Naples, Italy.
Valenti
Anna
A
D'amaro
Anna
A
Rossi
Mosè
M
Ciaramella
Maria
M
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
C041813:DNA reverse gyrase; D004264:DNA Topoisomerases, Type I