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J. Biol. Chem., Vol. 277, Issue 46, 44068-44078, November 15, 2002
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From the The availability of the complete genome sequence
of Bacillus subtilis has allowed the prediction of all
exported proteins of this Gram-positive eubacterium. Recently, ~180
secretory and 114 lipoprotein signal peptides were predicted to direct
protein export from the cytoplasm. Whereas most exported proteins
appear to use the Sec pathway, 69 of these proteins could potentially use the Tat pathway, as their signal peptides contain RR- or KR-motifs. In the present studies, proteomic techniques were applied to verify how
many extracellular B. subtilis proteins follow the Tat
pathway. Strikingly, the extracellular accumulation of 13 proteins with potential RR/KR-signal peptides was Tat-independent, showing that their
RR/KR-motifs are not recognized by the Tat machinery. In fact, only the
phosphodiesterase PhoD was shown to be secreted in a strictly
Tat-dependent manner. Sodium azide-inhibition of SecA
strongly affected the extracellular appearance of de novo synthesized proteins, including the lipase LipA and two other proteins
with predicted RR/KR-signal peptides. The SecA-dependent export of pre-LipA is particularly remarkable, because its RR-signal peptide conforms well to stringent criteria for the prediction of
Tat-dependent export in Escherichia coli.
Taken together, our observations show that the Tat pathway makes
a highly selective contribution to the extracellular proteome of
B. subtilis.
Selective Contribution of the Twin-Arginine
Translocation Pathway to Protein Secretion in Bacillus
subtilis*
§,,,
**,,,§§, and
Department of Genetics, Groningen
Biomolecular Sciences and Biotechnology Institute, Kerklaan 30, 9751 NN
Haren, The Netherlands, the ¶ Institut für Mikrobiologie und
Molekularbiologie, Ernst-Moritz-Arndt-Universität Greifswald,
F.-L.-Jahn-Strasse 15, D-17487 Greifswald, Germany, the National
Public Health Institute, Mannerheimintie 166, FIN-00300, Helsinki,
Finland, and the Department of
Pharmaceutical Biology, University of Groningen, A. Deusinglaan 1, 9713 AV Groningen, The Netherlands
*
This work was supported in part by "Quality of Life and
Management of Living Resources" Grants QLK3-CT-1999-00413 and
QLK3-CT-1999-00917 from the European Union (to J. D. H. J., H. A.,
M. H., P. G. B., S. B., W. J. Q., and J. M. v. D) and grants
from the "Deutsche Forschungsgemeinschaft" (DFG), the
"Bundesministerium für Bildung, Wissenschaft, Forschung und
Technologie" (BMFT), the "Fonds der Chemischen Industrie," and
Genencor International (to H. A. and M. H).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.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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