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. 1992 Apr;174(7):2305–2311. doi: 10.1128/jb.174.7.2305-2311.1992

Iron(III) hydroxamate transport in Escherichia coli K-12: FhuB-mediated membrane association of the FhuC protein and negative complementation of fhuC mutants.

G Schultz-Hauser 1, W Köster 1, H Schwarz 1, V Braun 1
PMCID: PMC205852  PMID: 1551849

Abstract

Iron(III) hydroxamate transport across the cytoplasmic membrane is catalyzed by the very hydrophobic FhuB protein and the membrane-associated FhuC protein, which contains typical ATP-binding domains. Interaction between the two proteins was demonstrated by immunoelectron microscopy with anti-FhuC antibodies, which showed FhuB-mediated association of FhuC with the cytoplasmic membrane. In addition, inactive FhuC derivatives carrying single amino acid replacements in the ATP-binding domains suppressed wild-type FhuC transport activity, which arose either from displacement of active FhuC from FhuB by the mutated FhuC derivatives or from the formation of mixed inactive FhuC multimers between wild-type and mutated FhuC proteins. Inactive FhuC derivatives containing internal deletions and insertions showed no phenotypic suppression, indicating conformational alterations that rendered the FhuC derivatives unable to displace wild-type FhuC. It is concluded that the physical interaction between FhuC and FhuB implies a coordinate activity of both proteins in the transport of iron(III) hydroxamates through the cytoplasmic membrane.

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Selected References

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