Energy coupling in type II topoisomerases: Why do they hydrolyze ATP?

被引:71
作者
Bates, Andrew D.
Maxwell, Anthony
机构
[1] Univ Liverpool, Sch Biol Sci, Liverpool L69 7ZB, Merseyside, England
[2] John Innes Ctr, Dept Biol Chem, Norwich NR4 7UH, Norfolk, England
关键词
COLI DNA GYRASE; N-TERMINAL FRAGMENT; LOCAL JUXTAPOSITION GEOMETRY; POSITIVELY SUPERCOILED DNA; STRAND-PASSAGE REACTION; NUCLEOTIDE-BINDING; MECHANISTIC ASPECTS; CRYSTAL-STRUCTURE; SINGLE-MOLECULE; OPERATED CLAMP;
D O I
10.1021/bi700789g
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Type II topoisomerases are essential enzymes in all cells. They help to solve the topological problems of DNA by passing one double helix through a transient break in another, in a reaction coupled to the hydrolysis of ATP. Members of one class of the enzymes, DNA gyrases, are configured to carry out an intramolecular reaction, removing positive supercoiling and introducing negative supercoiling into circular DNA using free energy derived from ATP hydrolysis. The nonsupercoiling class, including bacterial topoisomerase IV and eukaryotic topoisomerase II enzymes, can carry out both intra- and intermolecular reactions, and their primary role is the unlinking (decatenation) of daughter replicons before partition. In these enzymes, ATP hydrolysis is coupled to a reduction in DNA complexity (catenation, supercoiling, and knotting) below the level expected at equilibrium. This review discusses our current understanding of the mechanisms behind the coupling of the energy of ATP hydrolysis to topological changes catalyzed by both of these classes of enzyme.
引用
收藏
页码:7929 / 7941
页数:13
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