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J. Biol. Chem., Vol. 281, Issue 29, 19977-19984, July 21, 2006

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Affinity of TatC_d for TatA_d Elucidates Its Receptor Function in the Bacillus subtilis Twin Arginine Translocation (Tat) Translocase System^*

Sandra Schreiber, Rayk Stengel, Martin Westermann, Rudolph Volkmer-Engert^¶, Ovidiu I. Pop, and Jörg P. Müller¹

From the Institut für Molekulare Zellbiologie, Friedrich-Schiller-Universität Jena, Drackendorfer Strasse 1, D-07747 Jena, Germany, Elektronenmikroskopisches Zentrum, Klinikum der Friedrich-Schiller-Universität Jena, Ziegelmühlenweg 1, D-07743 Jena, Germany, and ^¶Abteilung für Molekulare Bibliotheken, Charite, Ziegelstrasse 5-9, 10117 Berlin, Germany

Twin arginine translocation (Tat) systems catalyze the transport of folded proteins across the bacterial cytosolic membrane or the chloroplast thylakoid membrane. In the Tat systems of Escherichia coli and many other species TatA-, TatB-, and TatC-like proteins have been identified as essential translocase components. In contrast, the Bacillus subtilis phosphodiesterase PhoD-specific system consists only of a pair of TatA_d/TatC_d proteins and involves a TatA_d protein engaged in a cytosolic and a membrane-embedded localization. Because soluble TatA_d was able to bind the twin arginine signal peptide of prePhoD prior to membrane integration it could serve to recruit its substrate to the membrane via the interaction with TatC_d. By analyzing the distribution of TatA_d and studying the mutual affinity with TatC_d we have shown here that TatC_d assists the membrane localization of TatA_d. Besides detergent-solubilized TatC_d, membrane-integrated TatC_d showed affinity for soluble TatA_d. By using a peptide library-specific binding of TatA_d to cytosolic loops of membrane protein TatC_d was demonstrated. Depletion of TatC_d in B. subtilis resulted in a drastic reduction of TatA_d, indicating a stabilizing effect of TatC_d for TatA_d. In addition, the presence of the substrate prePhoD was the prerequisite for appropriate localization in the cytosolic membrane of B. subtilis as demonstrated by freeze-fracture experiments.

Received for publication, December 30, 2005 , and in revised form, May 12, 2006.

^* This work was supported by the Deutsche Forschungsgemeinschaft. 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.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Fig. S1.

¹ To whom correspondence should be addressed. Tel.: 49-3641-9325671; Fax: 49-3641-9325652; E-mail: joerg.mueller2{at}med.uni-jena.de.

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