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

Schultz-Hauser, Gabriele; Köster, Wolfgang; Schwarz, Heinz; Braun, Volkmar

doi:10.1128/jb.174.7.2305-2311.1992

Cited by 24 publications

(16 citation statements)

References 35 publications

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“…The 'natural linker' combining the two major domains in wild-type FhuB is too short and too hydrophilic to act as a transmembrane segment, suggesting that the active protein has an even number of membrane-spanning regions with the N-and C-termini located on the same side of the membrane (Koster & Braun, 1990;Koster, 1991). Each half of FhuB contains a conserved region (CR) which is presumably involved in the interaction with FhuC (Schultz-Hauser et al, 1992;Bohm et al, 1996). A reliable topological model is an important prerequisite for the interpretation of existing data and for the design of further experiments to identify functional (sub)domains.…”

Section: Introductionmentioning

confidence: 99%

Transmembrane topology of the two FhuB domains representing the hydrophobic components of bacterial ABC transporters involved in the uptake of siderophores, haem and vitamin B

Groeger¹,

KOstert²

1998

Microbiology

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Transport of siderophores of the hydroxamate type across the Escherichia coli cytoplasmic membrane depends on a periplasmic binding-protein-dependent (PBT) system. This uptake system consists of the binding protein FhUD, the membrane-associated putative ATP-hydrolase FhuC and the integral membrane protein FhuB. The two halves of FhuB [FhuB(N) and FhuB(C)], both essential for transport, are similar with respect to structure and function. Regions were identified in FhuB(N) and FhuB(C) which are presumably involved in the interaction of the two FhuB halves with each other or with other components of the uptake system, or with the different substrates. To determine the topology of the membrane-embedded polypeptide chain, FhuB'-'/?-lactamase protein fusions were analysed. The experimental data suggest that each half of the FhuB is able to fold autonomously into the lipid bilayer, which is a prerequisite for the assembly of both halves into a transport-competent formation. The hydrophobic components from PBT systems involved in the uptake of siderophores, haem and vitamin B, , define a subclass of polytopic integral membrane proteins. The topology of these 'siderophore family' proteins differs from that of the equivalent components of other PBT systems in that each polypeptide (and each half of FhuB) consists of 10 membranespanning regions, with the N-and C-termini located in the cytoplasm. The conserved region a t a distance of about 90 amino acids from the C-terminus, typical of all hydrophobic PBT proteins, is also oriented to the cytoplasm. However, in the siderophore family' proteins this putative ATPase interaction loop is followed by four instead of two transmembrane spans.

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Section: Introductionmentioning

confidence: 99%

Transmembrane topology of the two FhuB domains representing the hydrophobic components of bacterial ABC transporters involved in the uptake of siderophores, haem and vitamin B

Groeger¹,

KOstert²

1998

Microbiology

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“…Proteins involved in uptake of iron citrate and iron DFOB are induced in iron-starved P. aeruginosa (34,36). Ferric citrate was also shown to be an iron source for Escherichia coli along with the siderophores enterobactin and ferric hydroxamate (18,46). Staphylococcus aureus uses siderophores such as staphyloferrins A and B and staphylobactin and additionally possesses the capacity for ferric hydroxamate uptake.…”

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confidence: 99%

The Antibacterial Activity of Ga³⁺Is Influenced by Ligand Complexation as Well as the Bacterial Carbon Source

Rzhepishevska

Ekstrand‐Hammarström

Popp

et al. 2011

Antimicrob Agents Chemother

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Gallium ions have previously been shown to exhibit antibacterial and antibiofilm properties. In this study, we report differential bactericidal activities of two gallium complexes, gallium desferrioxamine B (Ga-DFOB) and gallium citrate (Ga-Cit). Modeling of gallium speciation in growth medium showed that DFOB and citrate both can prevent precipitation of Ga(OH) 3 , but some precipitation can occur above pH 7 with citrate. Despite this, Ga-Cit 90% inhibitory concentrations (IC 90 ) were lower than those of Ga-DFOB for clinical isolates of Pseudomonas aeruginosa and several reference strains of other bacterial species. Treatment with Ga compounds mitigated damage inflicted on murine J774 macrophage-like cells infected with P. aeruginosa PAO1. Again, Ga-Cit showed more potent mitigation than did Ga-DFOB. Ga was also taken up more efficiently by P. aeruginosa in the form of Ga-Cit than in the form of Ga-DFOB. Neither Ga-Cit nor Ga-DFOB was toxic to several human cell lines tested, and no proinflammatory activity was detected in human lung epithelial cells after exposure in vitro. Metabolomic analysis was used to delineate the effects of Ga-Cit on the bacterial cell. Exposure to Ga resulted in lower concentrations of glutamate, a key metabolite for P. aeruginosa, and of many amino acids, indicating that Ga affects various biosynthesis pathways. An altered protein expression profile in the presence of Ga-Cit suggested that some compensatory mechanisms were activated in the bacterium. Furthermore, the antibacterial effect of Ga was shown to vary depending on the carbon source, which has importance in the context of medical applications of gallium.

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“…Taken together, these results suggest that FhuD functions as a carrier protein; ferrichrome released from the OM receptor is delivered by FhuD to the permease. The integral membrane protein FhuB then translocates the siderophore into the cytoplasm mediated by ATP hydrolysis of FhuC (11).…”

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confidence: 99%

Interactions between TonB from Escherichia coli and the Periplasmic Protein FhuD

Carter

Miousse

Gagnon

et al. 2006

Journal of Biological Chemistry

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

Abstract: (8,9,16,28). These iron hydroxamates are transported across the cytoplasmic membrane by the same transport system composed of the periplasmic FhuD protein, the very hydrophobic transmembrane FhuB protein, and the membrane-associated FhuC protein (8,10,11,16,23,24

Cited by 24 publications

References 35 publications

Transmembrane topology of the two FhuB domains representing the hydrophobic components of bacterial ABC transporters involved in the uptake of siderophores, haem and vitamin B

Transmembrane topology of the two FhuB domains representing the hydrophobic components of bacterial ABC transporters involved in the uptake of siderophores, haem and vitamin B

The Antibacterial Activity of Ga³⁺Is Influenced by Ligand Complexation as Well as the Bacterial Carbon Source

Interactions between TonB from Escherichia coli and the Periplasmic Protein FhuD

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

Abstract: (8,9,16,28). These iron hydroxamates are transported across the cytoplasmic membrane by the same transport system composed of the periplasmic FhuD protein, the very hydrophobic transmembrane FhuB protein, and the membrane-associated FhuC protein (8,10,11,16,23,24

Cited by 24 publications

References 35 publications

Transmembrane topology of the two FhuB domains representing the hydrophobic components of bacterial ABC transporters involved in the uptake of siderophores, haem and vitamin B

Transmembrane topology of the two FhuB domains representing the hydrophobic components of bacterial ABC transporters involved in the uptake of siderophores, haem and vitamin B

The Antibacterial Activity of Ga3+Is Influenced by Ligand Complexation as Well as the Bacterial Carbon Source

Interactions between TonB from Escherichia coli and the Periplasmic Protein FhuD

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The Antibacterial Activity of Ga³⁺Is Influenced by Ligand Complexation as Well as the Bacterial Carbon Source