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J. Biol. Chem., Vol. 278, Issue 40, 38428-38436, October 3, 2003

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Sequence-specific Binding of prePhoD to Soluble TatA_d Indicates Protein-mediated Targeting of the Tat Export in Bacillus subtilis^*,

Ovidiu I. Pop , Martin Westermann , Rudolf Volkmer-Engert ¶, Daniela Schulz ¶, Cornelius Lemke ||, Sandra Schreiber , Roman Gerlach  **, Reinhard Wetzker  and Jörg P. Müller  

From the Institut für Molekularbiologie, Friedrich-Schiller-Universität Jena, Hans-Knöll-Strasse 2, Jena D-07745, Germany, Institut für Ultrastrukturforschung, Klinikum der Friedrich-Schiller-Universität Jena, Ziegelmühlenweg 1, Jena D-07743, Germany, ^¶Abt. f. Molekulare Bibliotheken, Charite, Ziegelstr. 5–9, Berlin 10117, Germany, ^||Institut für Anatomie 1, Friedrich-Schiller-Universität Jena, Teichgraben 7, Jena 07743, Germany, and Arbeitsgruppe Molekulare Zellbiologie, Klinikum der Friedrich-Schiller-Universität Jena, Drackendorfer Strasse 1, Jena D-07747, Germany

The Tat (twin-arginine protein translocation) system initially discovered in the thylakoid membrane of chloroplasts has been described recently for a variety of eubacterial organisms. Although in Escherichia coli four Tat proteins with calculated membrane spanning domains have been demonstrated to mediate Tat-dependent transport, a specific transport system for twin-arginine signal peptide containing phosphodiesterase PhoD of Bacillus subtilis consists of one TatA/TatC (TatA_d/TatC_d) pair of proteins. Here, we show that TatA_d was found beside its membrane-integrated localization in the cytosol were it interacted with prePhoD. prePhoD was efficiently co-immunoprecipitated by TatA_d. Inefficient co-immunoprecipitation of mature PhoD and missing interaction to Sec-dependent and cytosolic peptides by TatA_d demonstrated a particular role of the twin-arginine signal peptide for this interaction. Affinity of prePhoD to TatA_d was interfered by peptides containing the twin-arginine motif but remained active when the arginine residues were substituted. The selective binding of TatA_d to peptides derived from the signal peptide of PhoD elucidated the function of the twin-arginine motif as a target site for pre-protein TatA_d interaction. Substitution of the binding motif demonstrated the pivotal role of basic amino acid residues for TatA binding. These features suggest that TatA interacts prior to membrane integration with its pre-protein substrate and could therefore assist targeting of twin-arginine pre-proteins.

Received for publication, June 19, 2003 , and in revised form, July 15, 2003.

^* 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 figures.

^** Present address: Friedrich-Alexander-Universität Erlangen-Nürnberg, Institut für Klinische Mikrobiologie, Immunologie und Hygiene, Wasserturmstrasse 3–5, 91054 Erlangen, Germany.

To whom correspondence should be addressed. Tel.: 49-3641-657577; Fax: 49-3641-657520; E-mail: jmueller{at}imb-jena.de.

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