PMID:8100348
| Citation |
Karlsson, M, Hannavy, K and Higgins, CF (1993) ExbB acts as a chaperone-like protein to stabilize TonB in the cytoplasm. Mol. Microbiol. 8:389-96 |
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| Abstract |
The TonB protein is required to transduce energy from the cytoplasmic membrane to outer membrane transport proteins of Gram-negative bacteria. Two accessory proteins, ExbB and ExbD, are required for TonB function and it has been suggested that TonB and ExbBD form a complex in the membrane. In this paper we demonstrate that there are two spatially distinct, functional interactions between ExbBD and TonB. First, there is an interaction between ExbBD and the N-terminal signal-like peptide of TonB, probably the formation of a stable complex in the membrane. Second, ExbB interacts with TonB in the cytoplasm. This interaction involves the domain of TonB that is normally periplasmic. Thus, this is a transient interaction which occurs during the synthesis and/or localization of TonB, implying a chaperone-like role for ExbB. The transmembrane topology of ExbB was shown to be consistent with this role. |
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| Keywords |
Amino Acid Sequence; Bacterial Proteins/metabolism; Biological Transport; Chaperonins; Cytoplasm/metabolism; Energy Metabolism; Escherichia coli/metabolism; Escherichia coli Proteins; Membrane Proteins/metabolism; Molecular Sequence Data; Protein Conformation; Protein Processing, Post-Translational; Proteins/metabolism; Recombinant Fusion Proteins/metabolism |
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