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Journal of Bacteriology, January 2004, p. 366-373, Vol. 186, No. 2
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.2.366-373.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Phage Shock Protein PspA of Escherichia coli Relieves Saturation of Protein Export via the Tat Pathway

Department of Chemical Engineering,¹ Institute for Cell and Molecular Biology,² Department of Biomedical Engineering, University of Texas, Austin, Texas 78712,⁴ Department of Molecular Microbiology, John Innes Centre, Norwich, Norfolk NR4 7UH, United Kingdom³

Received 15 July 2003/ Accepted 10 October 2003

Overexpression of either heterologous or homologous proteins that are routed to the periplasm via the twin-arginine translocation (Tat) pathway results in a block of export and concomitant accumulation of the respective protein precursor in the cytoplasm. Screening of a plasmid-encoded genomic library for mutants that confer enhanced export of a TorA signal sequence (ssTorA)-GFP-SsrA fusion protein, and thus result in higher cell fluorescence, yielded the pspA gene encoding phage shock protein A. Coexpression of pspA relieved the secretion block observed with ssTorA-GFP-SsrA or upon overexpression of the native Tat proteins SufI and CueO. A similar effect was observed with the Synechocystis sp. strain PCC6803 PspA homologue, VIPP1, indicating that the role of PspA in Tat export may be phylogenetically conserved. Mutations in Tat components that completely abolish export result in a marked induction of PspA protein synthesis, consistent with its proposed role in enhancing protein translocation via Tat.

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