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J. Biol. Chem., Vol. 281, Issue 10, 6850-6859, March 10, 2006

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ATP Hydrolysis Is Essential for the Function of the Uup ATP-binding Cassette ATPase in Precise Excision of Transposons^*

Dorothée Murat¹, Pierre Bance, Isabelle Callebaut, and Elie Dassa²

From the Unité des Membranes Bactériennes CNRS URA2172, Département de Microbiologie Fondamentale et Médicale, Site Fernbach, Institut Pasteur, 25 Rue du Docteur Roux, 75724 Paris Cedex 15, France and the Département de Biologie Structurale, Institut de Minéralogie et de Physique des Milieux Condensés, CNRS UMR C7590, UP6 and UP7, Case 115, 4 Place Jussieu, 75252 Paris Cedex 05, France

In Escherichia coli K-12, the RecA- and transposase-independent precise excision of transposons is thought to be mediated by the slippage of the DNA polymerase between the two short direct repeats that flank the transposon. Inactivation of the uup gene, encoding an ATP-binding cassette (ABC) ATPase, led to an important increase in the frequency of precise excision of transposons Tn10 and Tn5 and a defective growth of bacteriophage Mu. To provide insight into the mechanism of Uup in transposon excision, we purified this protein, and we demonstrated that it is a cytosolic ABC protein. Purified recombinant Uup binds and hydrolyzes ATP and undergoes a large conformational change in the presence of this nucleotide. This change affects a carboxyl-terminal domain of the protein that displays predicted structural homology with the socalled little finger domain of Y family DNA polymerases. In these enzymes, this domain is involved in DNA binding and in the processivity of replication. We show that Uup binds to DNA and that this binding is in part dependent on its carboxyl-terminal domain. Analysis of Walker motif B mutants suggests that ATP hydrolysis at the two ABC domains is strictly coordinated and is essential for the function of Uup in vivo.

Received for publication, September 8, 2005 , and in revised form, December 21, 2005.

^* 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.

¹ Supported by a fellowship from the Ministère délégué à l'Enseignement Supérieur et à la Recherche.

² To whom correspondence should be addressed: Unité des Membranes Bactériennes CNRS URA2172, Département de Microbiologie Fondamentale et Médicale, Site Fernbach, Inst. Pasteur, 25 Rue du Docteur Roux, 75724 Paris Cedex 15, France. Tel.: 33-1-45-68-88-31; Fax: 33-1-45-68-87-90; E-mail: elidassa{at}pasteur.fr.

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