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J. Bacteriol., 12 1997, 7274-7279, Vol 179, No. 23
Copyright © 1997, American Society for Microbiology

The TolB protein interacts with the porins of Escherichia coli

A Rigal, E Bouveret, R Lloubes, C Lazdunski and H Benedetti
Laboratoire d'Ingenierie et de Dynamique des Macromolecules, Institut de Biologie Structurale et Microbiologie, Centre National de la Recherche Scientifique, Marseille, France.

TolB is a periplasmic protein of the cell envelope Tol complex. It is partially membrane associated through an interaction with the outer membrane lipoprotein PAL (peptidoglycan-associated lipoprotein), which also belongs to the Tol system. The interaction of TolB with outer membrane porins of Escherichia coli was investigated with a purified TolB derivative harboring a six-histidine tag. TolB interacted with the trimeric porins OmpF, OmpC, PhoE, and LamB but not with their denatured monomeric forms or OmpA. These interactions took place both in the presence and in the absence of lipopolysaccharide. TolA, an inner membrane component of the Tol system, also interacts with the trimeric porins via its central periplasmic domain (R. Derouiche, M. Gavioli, H. Benedetti, A. Prilipov, C. Lazdunski, and R. Lloubes, EMBO J. 15:6408- 6415, 1996). In the presence of the purified central domain of TolA (TolAIIHis), the TolB-porin complexes disappeared to form TolAIIHis- porin complexes. These results suggest that the interactions of TolA and TolB with porins might take place in vivo and might be concomitant events participating in porin assembly. They also suggest that the Tol system as a whole may be involved in porin assembly in the outer membrane.


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