The role of ATP in the reactions of type II DNA topoisomerases

Author:

Bates Andrew D.1,Maxwell Anthony2

Affiliation:

1. School of Biological Sciences, University of Liverpool, Crown Street, Liverpool L69 7ZB, U.K.

2. Department of Biological Chemistry, John Innes Centre, Colney, Norwich NR4 7UH, U.K.

Abstract

Type II DNA topoisomerases catalyse changes in DNA topology in reactions coupled to the hydrolysis of ATP. In the case of DNA gyrase, which can introduce supercoils into DNA, the requirement for free energy is clear. However, the non-supercoiling type II enzymes carry out reactions that are apparently energetically favourable, so their requirement for ATP hydrolysis is not so obvious. It has been shown that many of these enzymes (the type IIA family) can simplify the topology of their DNA substrates to a level beyond that expected at equilibrium. Although this seems to explain their usage of ATP, we show that the free energies involved in topology simplification are very small (<0.2% of that available from ATP) and we argue that topology simplification may simply be an evolutionary relic.

Publisher

Portland Press Ltd.

Subject

Biochemistry

Reference22 articles.

1. DNA Topology;Bates,2005

2. DNA topoisomerases: structure, function, and mechanism;Champoux;Annu. Rev. Biochem.,2001

3. DNA topoisomerases: harnessing and constraining energy to govern chromosome topology;Schoeffler;Q. Rev. Biophys.,2008

4. DNA topoisomerases;Wang;Annu. Rev. Biochem.,1996

5. Energy coupling in type II topoisomerases: why do they hydrolyze ATP?;Bates;Biochemistry,2007

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