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J. Biol. Chem., Vol. 281, Issue 3, 1532-1546, January 20, 2006

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Formation of a Distinctive Complex between the Inducible Bacterial Lysine Decarboxylase and a Novel AAA+ ATPase^*

Jamie Snider1, Irina Gutsche2, Michelle Lin, Sabulal Baby, Brian Cox¶, Gareth Butland||, Jack Greenblatt||3, Andrew Emili||3, and Walid A. Houry4

From the Department of Biochemistry, University of Toronto, Toronto, Ontario M5S 1A8, Canada, the ^¶Samuel Lunenfeld Research Institute, Mount Sinai Hospital and Department of Medical Genetics and Microbiology, University of Toronto, Toronto, Ontario M5S 1A8, Canada, the ^||Banting and Best Department of Medical Research and Department of Medical Genetics and Microbiology, University of Toronto, Toronto, Ontario M5S 1A8, Canada, and the Laboratoire de Virologie Moléculaire et Structurale, UMR 2472/1157, CNRS-Institut National de la Recherche Agronomique and Institut Fédératif de Recherche 115, 1 Avenue de la Terrasse, 91198 Gif-sur-Yvette Cedex, France

AAA+ ATPases are ubiquitous proteins that employ the energy obtained from ATP hydrolysis to remodel proteins, DNA, or RNA. The MoxR family of AAA+ proteins is widespread throughout bacteria and archaea but is largely uncharacterized. Limited work with specific members has suggested a potential role as molecular chaperones involved in the assembly of protein complexes. As part of an effort aimed at determining the function of novel AAA+ chaperones in Escherichia coli, we report the characterization of a representative member of the MoxR family, YieN, which we have renamed RavA (regulatory ATPase variant A). We show that the ravA gene exists on an operon with another gene encoding a protein, YieM, of unknown function containing a Von Willebrand Factor Type A domain. RavA expression is under the control of the ^S transcription factor, and its levels increase toward late log/early stationary phase, consistent with its possible role as a general stress-response protein. RavA functions as an ATPase and forms hexameric oligomers. Importantly, we demonstrate that RavA interacts strongly with inducible lysine decarboxylase (LdcI or CadA) forming a large cage-like structure consisting of two LdcI decamers linked by a maximum of five RavA oligomers. Surprisingly, the activity of LdcI does not appear to be affected by binding to RavA in a number of in vitro and in vivo assays, however, complex formation results in the stimulation of RavA ATPase activity. Data obtained suggest that the RavA-LdcI interaction may be important for the regulation of RavA activity against its targets.

Received for publication, October 13, 2005

^* This work was supported in part by a grant from the Natural Sciences and Engineering Research Council of Canada (to W. A. H.). 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 Recipient of a graduate fellowship from the Natural Sciences and Engineering Research Council of Canada.

³ Supported by the Ontario Genomics Institute and Genome Canada.

² To whom questions regarding EM methodology should be addressed: IVMS, c/o EMBL Grenoble Outstation 38042 Grenoble Cedex 9, France. E-mail: gutsche{at}emblgrenoble.fr. ⁴ A Canadian Institutes of Health Research New Investigator. To whom correspondence should be addressed: 1 King's College Circle, Medical Sciences Bldg., Dept. of Biochemistry, University of Toronto, Toronto, Ontario M5S 1A8, Canada. Tel.: 416-946-7141; Fax: 416-978-8548; E-mail: walid.houry{at}utoronto.ca.

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