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Journal of Bacteriology, January 2001, p. 139-144, Vol. 183, No. 1
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.1.139-144.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Escherichia coli Strains Blocked in Tat-Dependent Protein Export Exhibit Pleiotropic Defects in the Cell Envelope

Nicola R. Stanley,1,2 Kim Findlay,3 Ben C. Berks,1 and Tracy Palmer1,2,*

Centre for Metalloprotein Spectroscopy and Biology, School of Biological Sciences, University of East Anglia, Norwich NR4 7TJ,1 and Departments of Molecular Microbiology2 and Cell Biology,3 John Innes Centre, Norwich NR4 7UH, United Kingdom

Received 23 August 2000/Accepted 26 September 2000

The Tat system is a recently discovered protein export pathway that serves to translocate folded proteins, often containing redox cofactors, across the bacterial cytoplasmic membrane. Here we report that tat strains are associated with a mutant cell septation phenotype, where chains of up to 10 cells are evident. Mutant strains are also hypersensitive to hydrophobic drugs and to lysis by lysozyme in the absence of EDTA, and they leak periplasmic enzymes, characteristics that are consistent with an outer membrane defect. Both phenotypes are similar to those displayed by strains carrying point mutations in the lpxC (envA) gene. The phenotype was not replicated by mutations affecting synthesis and/or activity of all known or predicted Tat substrates.

* Corresponding author. Mailing address: Department of Molecular Microbiology, John Innes Centre, Norwich NR4 7UH, United Kingdom. Phone: 44 (0)1603 450726. Fax: 44 (0)1603 450018. E-mail: tracy.palmer{at}bbsrc.ac.uk.

Journal of Bacteriology, January 2001, p. 139-144, Vol. 183, No. 1
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.1.139-144.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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