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J. Biol. Chem., Vol. 279, Issue 46, 47543-47554, November 12, 2004

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Novel Phenotypes of Escherichia coli tat Mutants Revealed by Global Gene Expression and Phenotypic Analysis^*

Bérengère Ize, Ida Porcelli¶||, Sacha Lucchini**, Jay C. Hinton**, Ben C. Berks¶, and Tracy Palmer

From the Department of Molecular Microbiology, John Innes Centre, Norwich NR4 7UH, United Kingdom, the School of Biological Sciences, University of East Anglia, Norwich NR4 7TJ, United Kingdom, the ^¶Department of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom, and the ^**Molecular Microbiology Group, Institute of Food Research, Norwich Research Park, Norwich NR4 7UA, United Kingdom

The Tat protein export system serves to export folded proteins harboring an N-terminal twin arginine signal peptide across the cytoplasmic membrane. In this study, we have used gene expression profiling of Escherichia coli supported by phenotypic analysis to investigate how cells respond to a defect in the Tat pathway. Previous work has demonstrated that strains mutated in genes encoding essential Tat pathway components are defective in the integrity of their cell envelope because of the mislocalization of two amidases involved in cell wall metabolism (Ize, B., Stanley, N. R., Buchanan, G., and Palmer, T. (2003) Mol. Microbiol. 48, 1183–1193). To distinguish between genes that are differentially expressed specifically because of the cell envelope defect and those that result from other effects of the tatC deletion, we also analyzed two different transposon mutants of the tatC strain that have their outer membrane integrity restored. Approximately 50% of the genes that were differentially expressed in the tatC mutant are linked to the envelope defect, with the products of many of these genes involved in self-defense or protection mechanisms, including the production of exopolysaccharide. Among the changes that were not explicitly linked to envelope integrity, we characterized a role for the Tat system in iron acquisition and copper homeostasis. Finally, we have demonstrated that overproduction of the Tat substrate SufI saturates the Tat translocon and produces effects on global gene expression that are similar to those resulting from the tatC mutation.

Received for publication, June 21, 2004 , and in revised form, August 11, 2004.

Note Added in Proof—Supplemental Table SI may also be downloaded from the following Web address: www.jic.bbsrc.au.uk/staff/tracy-palmer/.

^* This work was in part supported by Grant 83/P16414 and a core strategic grant from the Biotechnology and Biological Sciences Research Council (to J. C. H.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains Supplemental Table SI.

^|| Supported by a Ph.D. studentship from the Department of Biochemistry, University of Oxford.

Royal Society Research Fellow. To whom correspondence should be addressed: Dept. of Molecular Microbiology, John Innes Centre, Colney Lane, Norwich NR4 7UH, UK. Tel.: 44-1603-450726; Fax: 44-1603-450778; E-mail: tracy.palmer{at}bbsrc.ac.uk.

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