Peptidoglycan-associated lipoprotein-TolB interaction. A possible key to explaining the formation of contact sites between the inner and outer membranes of Escherichia coli

Abstract : TolA, -B, -Q, and -R proteins are involved in maintaining the cell envelope integrity of Escherichia coli; they have been parasitized by the group A colicins and the single strand DNA of some filamentous bacteriophages to permit them to enter the cells. TolA and TolR are anchored to the inner membrane by a single transmembrane domain, TolQ is an integral membrane protein with three transmembrane segments, and TolB has recently been found to be periplasmic although it is partially membrane-associated. The latter result suggests that TolB might interact with membrane proteins. Other lines of evidence favor the existence of a Tol complex. To further characterize this complex, we investigated which proteins interact with TolB. For this purpose, two different methods were used. First, we took advantage of the existence of a tagged TolB (TolBep) to perform immunoprecipitation under native conditions in order to preserve the putative associations of TolBep with other proteins. Secondly, in vivo cross-linking experiments with formaldehyde were performed. These two approaches led to the same result and demonstrated for the first time that a component of the Tol system, TolB, interacts with a protein located in the outer membrane, the peptidoglycan-associated lipoprotein.
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E. Bouveret, R Derouiche, R. Rigal, R Lloubès, C Lazdunski, et al.. Peptidoglycan-associated lipoprotein-TolB interaction. A possible key to explaining the formation of contact sites between the inner and outer membranes of Escherichia coli. Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 1995, 270 (19), pp.11071-11077. ⟨10.1074/jbc.270.19.11071⟩. ⟨hal-02130195⟩

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