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J. Biol. Chem., Vol. 279, Issue 24, 25783-25788, June 11, 2004

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The Path of the DNA along the Dimer Interface of Topoisomerase II^*

Joaquim Roca

From the Instituto de Biología Molecular de Barcelona, Consejo Superior de Investigaciones Científicas, Jordi Girona 18-26, 08034 Barcelona, Spain

The eukaryotic DNA topoisomerase II is a dyadic enzyme that, upon ATP binding, transports one duplex DNA (T-segment) through a transient double-stranded break in another (G-segment). The path of the T-segment involves the sequential crossing of three gates along the dimer interface: the entrance or N-gate, the DNA gate, and the exit or C-gate. Coordination among these gates is critical for dimer stability and the prevention of chromosome damage. This study examines DNA transactions by yeast topoisomerase II derivatives defective in gate function. The results indicate that, although the N-gate is not required for G-segment cleavage, the DNA gate per se is not able to widen unless ATP binds to the N-gate. Next, a captured T-segment cannot be held in the interdomainal region between the N-gate and the DNA gate. Finally, the G-segment can be religated while a T-segment is held in the central cavity of the enzyme between the DNA gate and the C-gate. These quaternary couplings for gate opening and closing suggest that topoisomerase II ensures a transient DNA gating state, during which dimer interface contacts are maximized and backtracking of the transported DNA is minimized.

Received for publication, March 5, 2004

^* This study was supported by Grants PB98-0487 and BMC2002-03275 from the Spanish Ministry of Science and Technology. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed. Tel.: 34-93-4006178; Fax: 34-93-2045904; E-mail: jrbbmc{at}cid.csic.es.

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