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(Received for publication, July 16, 1997, and in revised form, September 9, 1997)
From the The ferrichrome-iron receptor of
Escherichia coli is FhuA, an outer membrane protein that is
dependent upon the energy-coupling protein TonB to enable active
transport of specific hydroxamate siderophores, infection by certain
phages, and cell killing by the protein antibiotics colicin M and
microcin 25. In vivo cross-linking studies were performed
to establish at the biochemical level the interaction between FhuA and
TonB. In an E. coli strain in which both proteins were
expressed from the chromosome, a high molecular mass complex was
detected when the ferrichrome homologue ferricrocin was added
immediately prior to addition of cross-linker. The complex included
both proteins; it was absent from strains of E. coli that
were devoid of either FhuA or TonB, and it was detected with anti-FhuA
and anti-TonB monoclonal antibodies. These results indicate that,
in vivo, the binding of ferricrocin to FhuA enhances
complex formation between the receptor and TonB. An in
vitro system was established with which to examine the FhuA-TonB
interaction. Incubation of TonB with histidine-tagged FhuA followed by
addition of Ni2+-nitrilotriacetate-agarose led to the
specific recovery of both TonB and FhuA. Addition of ferricrocin or
colicin M to FhuA in this system greatly increased the coupling between
FhuA and TonB. Conversely, a monoclonal antibody that binds near the N
terminus of FhuA reduced the retention of TonB by histidine-tagged
FhuA. These studies demonstrate the significance of ligand binding at the external surface of the cell to mediate signal transduction across
the outer membrane.
Volume 272, Number 45,
Issue of November 7, 1997
pp. 28391-28397
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
Cell Envelope Signaling in Escherichia coli
LIGAND BINDING TO THE FERRICHROME-IRON RECEPTOR FhuA PROMOTES
INTERACTION WITH THE ENERGY-TRANSDUCING PROTEIN TonB
,
and
Department of Microbiology and Immunology,
McGill University, Montreal, Quebec H3A 2B4, Canada and the
Department of Microbiology and Department of Biochemistry and
Biophysics, Washington State University,
Pullman, Washington 99164-4233
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