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J. Biol. Chem., Vol. 280, Issue 36, 31378-31389, September 9, 2005

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XcpX Controls Biogenesis of the Pseudomonas aeruginosa XcpT-containing Pseudopilus^*

Éric Durand, Gérard Michel, Romé Voulhoux, Julia Kürner¶, Alain Bernadac, and Alain Filloux||

From the Laboratoire d'Ingénierie des Systèmes Macromoléculaires, UPR9027, IBSM/CNRS, 31 Chemin Joseph Aiguier, 13402 Marseille Cedex 20, France and the ^¶Department of Structural Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18a, D-82152 Martinsried, Germany

Pseudomonas aeruginosa is an opportunistic Gram-negative pathogen equipped with multiple secretion systems. The type II secretion machinery (Xcp secreton) is involved in the release of toxins and enzymes. The Xcp secreton is a multiprotein complex, and most of its components share homology with proteins involved in type IV pili biogenesis. Among them, the XcpT-X pseudopilins possess characteristics of the major constituent of the type IV pili, the pilin PilA. We have shown previously that XcpT can be assembled in a multifibrillar structure that was called the pseudopilus. By using two different microscopic approaches, we show here that the pseudopili are preferentially isolated fibers rather than tight bundles. Moreover, none of the other four pseudopilins are able to form a pseudopilus, suggesting that the assembly of such a structure is a unique property of XcpT. Moreover, we show that 5 of the 12 Xcp proteins are not required for pseudopilus biogenesis, whereas they are for type II secretion. Most interestingly, we showed that one pseudopilin, XcpX, controls the assembly of XcpT into a pseudopilus. Indeed, when the number of XcpX subunits increases, the length of the pseudopilus decreases. Conversely, in the absence of XcpX, the pseudopilus length is abnormally long. Our results indicate that XcpT and XcpX directly interact with each other. Furthermore, this interaction induces a clear destabilization of XcpT. The interaction between XcpT and XcpX could be part of the molecular mechanism underlying the dynamic control of pseudopilus elongation, which could be crucial for type II-dependent protein secretion.

Received for publication, May 27, 2005 , and in revised form, July 11, 2005.

^* This work was supported in part by European Union Grant QLK3CT-2002-02086. 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.

Supported by fellowships from the Ministère de l'Education Nationale de la Recherche et des Technologies and from the Fondation pour la Recherche Médicale.

^|| To whom correspondence should be addressed: Laboratoire d'Ingénierie des Systèmes Macromoléculaires, UPR9027, IBSM/CNRS, 31 Chemin Joseph Aiguier, 13402 Marseille Cedex 20, France. Tel.: 33-4-91164127; Fax: 33-4-91712124; E-mail: filloux{at}ibsm.cnrs-mrs.fr.

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