PMID:1551849
| Citation |
Schultz-Hauser, G, Köster, W, Schwarz, H and Braun, V (1992) Iron(III) hydroxamate transport in Escherichia coli K-12: FhuB-mediated membrane association of the FhuC protein and negative complementation of fhuC mutants. J. Bacteriol. 174:2305-11 |
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| 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. |
| Links | |
| Keywords |
Bacterial Proteins/metabolism; Base Sequence; Biological Transport; Carrier Proteins/metabolism; Cell Compartmentation; Escherichia coli/metabolism; Escherichia coli Proteins; Ferric Compounds/metabolism; Genetic Complementation Test; Hydroxamic Acids/metabolism; Membrane Proteins/metabolism; Membrane Transport Proteins; Molecular Sequence Data; Oligodeoxyribonucleotides/chemistry; Periplasmic Binding Proteins |
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