title: Coupling ATP hydrolysis to DNA strand passage in type IIA DNA topoisomerases.
abstract: Type IIA topos (topoisomerases) catalyse topological conversions of DNA through the passage of one double strand through a transient break in another. In the case of the archetypal enzyme, DNA gyrase, it has always been apparent that the enzyme couples the free energy of ATP hydrolysis to the introduction of negative supercoiling, and the structural details of this process are now becoming clearer. The homologous type IIA enzymes such as topo IV and eukaryotic topo II also require ATP and it has more recently been shown that the energy of hydrolysis is coupled to a reduction of supercoiling or catenation (linking) beyond equilibrium. The mechanism behind this effect is less clear. We review the energy coupling process in both classes of enzyme and describe recent mechanistic and structural work on gyrase that addresses the mechanism of energy coupling.
authors.affiliation: Department of Biological Chemistry, John Innes Centre, Colney, Norwich NR4 7UH, UK. tony.maxwell@bbsrc.ac.uk
authors.forename: A
authors.initials: A
authors.lastname: Maxwell
authors.forename: L
authors.initials: L
authors.lastname: Costenaro
authors.forename: S
authors.initials: S
authors.lastname: Mitelheiser
authors.forename: A D
authors.initials: AD
authors.lastname: Bates
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism*; D000818:Animals; D000951:Antigens, Neoplasm / Q000737:chemistry / Q000378:metabolism*; D004250:DNA Topoisomerases, Type II / Q000737:chemistry / Q000378:metabolism*; D004278:DNA, Superhelical / Q000737:chemistry / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D006868:Hydrolysis; D008957:Models, Genetic; D008958:Models, Molecular; D009690:Nucleic Acid Conformation; D011487:Protein Conformation
chemical_list: D000951:Antigens, Neoplasm; D004278:DNA, Superhelical; D004268:DNA-Binding Proteins; D000255:Adenosine Triphosphate; D004250:DNA Topoisomerases, Type II