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Journal of Bacteriology, February 2002, p. 754-759, Vol. 184, No. 3
0021-9193/01/$04.00+0     DOI: 10.1128/JB.184.3.754-759.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Pal Lipoprotein of Escherichia coli Plays a Major Role in Outer Membrane Integrity

Eric Cascales,1 Alain Bernadac,1 Marthe Gavioli,1 Jean-Claude Lazzaroni,2 and Roland Lloubes1*

Laboratoire d’Ingéniérie des Systèmes Macromoléculaires, Institut de Biologie Structurale et de Microbiologie, CNRS, UPR 9027, 31 Chemin Joseph Aiguier, 13402 Marseille Cedex 20,1 Unité de Microbiologie et Génétique CNRS-INSA-UCBL, UMR 5122, Université Claude Bernard Lyon 1, 69622 Villeurbanne Cedex, France2

Received 6 August 2001/ Accepted 3 November 2001

The Tol-Pal system of gram-negative bacteria is composed of five proteins. TolA, TolQ, and TolR are inner membrane proteins, TolB is a periplasmic protein, and Pal, the peptidoglycan-associated lipoprotein, is anchored to the outer membrane. In this study, the roles of Pal and major lipoprotein Lpp were compared in Escherichia coli. lpp and tol-pal mutations have previously been found to perturb the outer membrane permeability barrier and to cause the release of periplasmic proteins and the formation of outer membrane vesicles. In this study, we showed that the overproduction of Pal is able to restore the outer membrane integrity of an lpp strain but that overproduced Lpp has no effect in a pal strain. Together with the previously reported observation that overproduced TolA complements an lpp but not a pal strain, these results indicate that the cell envelope integrity is efficiently stabilized by an epistatic Tol-Pal system linking inner and outer membranes. The density of Pal was measured and found to be lower than that of Lpp. However, Pal was present in larger amounts compared to TolA and TolR proteins. The oligomeric state of Pal was determined and a new interaction between Pal and Lpp was demonstrated.

* Corresponding author. Mailing address: Laboratoire d’Ingéniérie des Systèmes Macromoléculaires, Institut de Biologie Structurale et de Microbiologie, CNRS, UPR 9027, 31 Chemin Joseph Aiguier, 13402 Marseille Cedex 20, France. Phone: (33) 4 91 16 46 63. Fax: (33) 4 91 71 21 24. E-mail: lloubes{at}ibsm.cnrs-mrs.fr.

Journal of Bacteriology, February 2002, p. 754-759, Vol. 184, No. 3
0021-9193/01/$04.00+0     DOI: 10.1128/JB.184.3.754-759.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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