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Biochem Soc Trans. 2005 Dec;33(Pt 6):1465-70.

Recent advances in understanding structure-function relationships in the type II topoisomerase mechanism.

Author information

1
Department of Molecular and Cell Biology, 237 Hildebrand Hall #3206, University of California, Berkeley, CA 94720-3206, USA.

Abstract

DNA topos (topoisomerases) are complex, multisubunit enzymes that remodel DNA topology. Members of the type II topo family function by passing one segment of duplex DNA through a transient break in another, a process that consumes two molecules of ATP and requires the co-ordinated action of multiple domains. Recent structural data on type II topo ATPase regions, which activate and enforce the directionality of DNA strand passage, have highlighted how ATP physically controls the catalytic cycle of the enzyme. Structural and biochemical studies of specialized DNA-binding domains in two paralogous bacterial type IIA topos (DNA gyrase and topo IV) show how these enzymes selectively negatively supercoil or decatenate DNA. Taken together, these findings expand our understanding of how disparate functional elements work together to co-ordinate the type II topo mechanism.

PMID:
16246147
DOI:
10.1042/BST20051465
[Indexed for MEDLINE]

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