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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
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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Copyright © 2000 by the American Society for Biochemistry and Molecular Biology.
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