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Originally published In Press as doi:10.1074/jbc.M004887200 on September 27, 2000

J. Biol. Chem., Vol. 275, Issue 52, 41350-41357, December 29, 2000
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TatC Is a Specificity Determinant for Protein Secretion via the Twin-arginine Translocation Pathway*

Jan D. H. Jongbloedabcd, Ulrike Martinbef, Haike Antelmanngh, Michael Heckerdgh, Harold Tjalsmaai, Gerard Venemaa, Sierd Bronad, Jan Maarten van Dijldjk, and Jörg Mülleref

From the a Department of Genetics, Groningen Biomolecular Sciences and Biotechnology Institute, Kerklaan 30, 9751 NN Haren, The Netherlands, the e Institute of Molecular Biology, Jena University, Winzerlaer Strasse 10, D-07745 Jena, Germany, the g Institut für Mikrobiologie und Molekularbiologie, Ernst-Moritz-Arndt-Universität Greifswald, F.-L.-Jahn-Strasse 15, D-17487 Greifswald, Germany, and the j Department of Pharmaceutical Biology, University of Groningen, A. Deusinglaan 1, 9713 AV Groningen, The Netherlands

The recent discovery of a ubiquitous translocation pathway, specifically required for proteins with a twin-arginine motif in their signal peptide, has focused interest on its membrane-bound components, one of which is known as TatC. Unlike most organisms of which the genome has been sequenced completely, the Gram-positive eubacterium Bacillus subtilis contains two tatC-like genes denoted tatCd and tatCy. The corresponding TatCd and TatCy proteins have the potential to be involved in the translocation of 27 proteins with putative twin-arginine signal peptides of which ~6-14 are likely to be secreted into the growth medium. Using a proteomic approach, we show that PhoD of B. subtilis, a phosphodiesterase belonging to a novel protein family of which all known members are synthesized with typical twin-arginine signal peptides, is secreted via the twin-arginine translocation pathway. Strikingly, TatCd is of major importance for the secretion of PhoD, whereas TatCy is not required for this process. Thus, TatC appears to be a specificity determinant for protein secretion via the Tat pathway. Based on our observations, we hypothesize that the TatC-determined pathway specificity is based on specific interactions between TatC-like proteins and other pathway components, such as TatA, of which three paralogues are present in B. subtilis.


* The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

b These authors contributed equally to this work.

c Supported by Grant 805-33.605 from the Stichting Levenswetenschappen.

d Supported by Quality of Life and Management of Living Resources Grants QLK3-CT-1999-00415 and QLK3-CT-1999-00917 from the European Union.

f Supported by the Deutsche Forschungsgemeinschaft.

h Supported by grants from the Deutsche Forschungsgemeinschaft; the Bundesministerium für Bildung, Wissenschaft, Forschung, und Technologie; and the Fonds der Chemischen Industrie.

i Supported by Genencor International (Leiden, The Netherlands).

k To whom correspondence should be addressed. Tel.: 31-50-3633079; Fax: 31-50-3636908; E-mail: j.m.van.dijl@farm.rug.nl.


Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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