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Clavel, T, Germon, P, Vianney, A, Portalier, R and Lazzaroni, JC (1998) TolB protein of Escherichia coli K-12 interacts with the outer membrane peptidoglycan-associated proteins Pal, Lpp and OmpA. Mol. Microbiol. 29:359-67
The Tol-Pal proteins of Escherichia coli are involved in maintaining outer membrane integrity. Transmembrane domains of TolQ, TolR and TolA interact in the cytoplasmic membrane, while TolB and Pal form a complex near the outer membrane. TolB and the central domain of TolA interact in vitro with the outer membrane porins. In this study, both genetic and biochemical analyses were carried out to analyse the links between TolB, Pal and other components of the cell envelope. It was shown that TolB could be cross-linked in vivo with Pal, OmpA and Lpp, while Pal was associated with TolB and OmpA. The isolation of pal and tolB mutants disrupting some interactions between these proteins represents at first approach to characterizing the residues contributing to the interactions. We propose that TolB and Pal are part of a multiprotein complex that links the peptidoglycan to the outer membrane. The Tol-Pal proteins might form transenvelope complexes that bring the two membranes into close proximity and help some outer membrane components to reach their final destination.
Amino Acid Sequence; Bacterial Outer Membrane Proteins/biosynthesis; Bacterial Outer Membrane Proteins/genetics; Bacterial Outer Membrane Proteins/metabolism; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Carrier Proteins/metabolism; Cross-Linking Reagents; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins; Lipoproteins/genetics; Lipoproteins/metabolism; Membrane Proteins/metabolism; Molecular Sequence Data; Mutagenesis; Peptidoglycan/genetics; Peptidoglycan/metabolism; Periplasmic Proteins; Proteoglycans; Sequence Homology, Amino Acid