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J. Biol. Chem., Vol. 277, Issue 5, 3268-3273, February 1, 2002

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The Twin-arginine Signal Peptide of PhoD and the TatA_d/C_d Proteins of Bacillus subtilis Form an Autonomous Tat Translocation System^*

Ovidiu Pop^§, Ulrike Martin^¶, Christian Abel, and Jörg P. Müller^§

From the Institutes of  Molecular Biology and ^¶ Virology, Jena University, Winzerlaer Str. 10, D-07745 Jena, Germany

The bacterial twin-arginine translocation (Tat) pathway has been recently described for PhoD of Bacillus subtilis, a phosphodiesterase containing a twin-arginine signal peptide. The expression of phoD is co-regulated with the expression of tatA_d and tatC_d genes localized downstream of phoD. To characterize the specificity of PhoD transport further, translocation of PhoD was investigated in Escherichia coli. By using gene fusions, we analyzed the particular role of the signal peptide and the mature region of PhoD in canalizing the transport route. A hybrid protein consisting of the signal peptide of -lactamase and mature PhoD was transported in a Sec-dependent manner indicating that the mature part of PhoD does not contain information canalizing the selected translocation route. Pre-PhoD, as well as a fusion protein consisting of the signal peptide of PhoD (SP_PhoD) and -galactosidase (LacZ), remained cytosolic in the E. coli. Thus, SP_PhoD is not recognized by E. coli transport systems. Co-expression of B. subtilis tatA_d/C_d genes resulted in the processing of SP_PhoD-LacZ and periplasmic localization of LacZ illustrating a close substrate specificity of the TatA_d/C_d transport system. While blockage of the Sec-dependent transport did not affect the localization of SP_PhoD-LacZ, translocation and processing was dependent on the pH gradient of the cytosolic membrane. Thus, the minimal requirement of a functional Tat-dependent protein translocation system consists of a twin-arginine signal peptide-containing Tat substrate, its specific TatA/C proteins, and the pH gradient across the cytosolic membrane.

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