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.
Skip Nav Destination
Article navigation
October 2005
-
Cover Image
Cover Image
- PDF Icon PDF LinkFront Matter
- PDF Icon PDF LinkTable of Contents
Conference Article|
October 26 2005
Recent advances in understanding structure–function relationships in the type II topoisomerase mechanism
A.J. Schoeffler;
A.J. Schoeffler
1Department of Molecular and Cell Biology, 237 Hildebrand Hall #3206, University of California, Berkeley, CA 94720-3206, U.S.A.
Search for other works by this author on:
J.M. Berger
J.M. Berger
1
1Department of Molecular and Cell Biology, 237 Hildebrand Hall #3206, University of California, Berkeley, CA 94720-3206, U.S.A.
1To whom correspondence should be addressed (email jmberger@berkeley.edu).
Search for other works by this author on:
Publisher: Portland Press Ltd
Received:
June 17 2005
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2005 The Biochemical Society
2005
Biochem Soc Trans (2005) 33 (6): 1465–1470.
Article history
Received:
June 17 2005
Citation
A.J. Schoeffler, J.M. Berger; Recent advances in understanding structure–function relationships in the type II topoisomerase mechanism. Biochem Soc Trans 26 October 2005; 33 (6): 1465–1470. doi: https://doi.org/10.1042/BST0331465
Download citation file:
Sign in
Don't already have an account? Register
Sign in to your personal account
You could not be signed in. Please check your email address / username and password and try again.
Could not validate captcha. Please try again.