ABC transporter-mediated uptake of iron, siderophores, heme and vitamin B12

Köster, Wolfgang

doi:10.1016/s0923-2508(01)01200-1

Cited by 238 publications

(200 citation statements)

References 28 publications

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“…Thus, the B 12 -specific components of the transporters are BtuBFCD and BtuFCD in Gram-negative and Gram-positive bacteria, respectively. The corresponding components of ABC transporters involved in the uptake of ferric siderophores, heme, and vitamin B 12 are similar and belong to the same families (32). Therefore, a similarity search is not sufficient to dissect the B 12 and ferric transporters in species distant from enteric bacteria.…”

Section: Conservedmentioning

confidence: 99%

Comparative Genomics of the Vitamin B12 Metabolism and Regulation in Prokaryotes

Rodionov

Vitreschak

Mironov

et al. 2003

Journal of Biological Chemistry

407

426

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Using comparative analysis of genes, operons, and regulatory elements, we describe the cobalamin (vitamin B 12 ) biosynthetic pathway in available prokaryotic genomes. Here we found a highly conserved RNA secondary structure, the regulatory B12 element, which is widely distributed in the upstream regions of cobalamin biosynthetic/transport genes in eubacteria. In addition, the binding signal (CBL-box) for a hypothetical B 12 regulator was identified in some archaea. A search for B12 elements and CBL-boxes and positional analysis identified a large number of new candidate B 12 -regulated genes in various prokaryotes. Among newly assigned functions associated with the cobalamin biosynthesis, there are several new types of cobalt transporters, ChlI and ChlD subunits of the CobN-dependent cobaltochelatase complex, cobalt reductase BluB, adenosyltransferase PduO, several new proteins linked to the lower ligand assembly pathway, L-threonine kinase PduX, and a large number of other hypothetical proteins. Most missing genes detected within the cobalamin biosynthetic pathways of various bacteria were identified as nonorthologous substitutes. The variable parts of the cobalamin metabolism appear to be the cobalt transport and insertion, the CobG/CbiG-and CobF/CbiD-catalyzed reactions, and the lower ligand synthesis pathway. The most interesting result of analysis of B12 elements is that B 12 -independent isozymes of the methionine synthase and ribonucleotide reductase are regulated by B12 elements in bacteria that have both B 12 -dependent and B 12 -independent isozymes. Moreover, B 12 regulons of various bacteria are thought to include enzymes from known B 12 -dependent or alternative pathways. Cobalamin (CBL),1 along with chlorophyll, heme, siroheme, and coenzyme F 430 , constitute a class of the most structurally complex cofactors synthesized by bacteria. The distinctive feature of these cofactors is their tetrapyrrole-derived framework with a centrally chelated metal ion (cobalt, magnesium, iron, or nickel). Methylcobalamin and Ado-CBL, two derivatives of vitamin B 12 (cyanocobalamin) with different upper axial ligands, are essential cofactors for several important enzymes that catalyze a variety of transmethylation and rearrangement reactions. Among the most prominent vitamin B 12 -dependent enzymes in bacteria and archaea are the methionine synthase isozyme MetH from enteric bacteria; the ribonucleotide reductase isozyme NrdJ from deeply rooted eubacteria and archaea; diol dehydratases and ethanolamine ammonia lyase from enteric bacteria involved in anaerobic glycerol, 1,2-propanediol, and ethanolamine fermentation; glutamate and methylmalonyl-CoA mutases from clostridia and streptomycetes; and various CBL-dependent methyltransferases from methane-producing archaea (1-5).Most prokaryotic organisms as well as animals (including humans) and protists have enzymes that require CBL as cofactor, whereas plants and fungi are thought not to use it. Among the CBL-utilizing organisms, only some bacterial and archaeal species ...

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Section: Conservedmentioning

confidence: 99%

Comparative Genomics of the Vitamin B12 Metabolism and Regulation in Prokaryotes

Rodionov

Vitreschak

Mironov

et al. 2003

Journal of Biological Chemistry

407

426

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“…ABC transporters involved in the transport of siderophores, heme, and vitamin B 12 cluster into a distinct family, and only a few bacterial species lack representatives of this transporter family (5). This family of proteins distinguishes itself from the majority of characterized binding proteins because the structure of proteins within this family lack the classic fold where the two domains of the bilobate structure are linked by a flexible hinge region that is comprised of ␤-strands at the base of the binding pocket.…”

Section: Fhud1 In S Aureusmentioning

confidence: 99%

“…Siderophores commonly bind ferric iron with extremely high affinities (4) and serve to solubilize iron from the biologically inert iron(III)-hydroxy precipitates. Typically, ferric-siderophores are mobilized across the cell envelope of Gram-negative bacteria expressing cognate outer membrane receptors, periplasmic-binding proteins, and associated ABC 1 -type transporters (5,6). In Gram-positive bacteria, ferric siderophores are captured by lipoproteins that function as high affinity receptors and subsequently feed ligand to the ABC transporter in the cytoplasmic membrane.…”

mentioning

confidence: 99%

FhuD1, a Ferric Hydroxamate-binding Lipoprotein in Staphylococcus aureus

Sebulsky

Speziali

Shilton

et al. 2004

Journal of Biological Chemistry

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Staphylococcus aureus can utilize ferric hydroxamates as a source of iron under iron-restricted growth conditions. Proteins involved in this transport process are: FhuCBG, which encodes a traffic ATPase; FhuD2, a post-translationally modified lipoprotein that acts as a high affinity receptor at the cytoplasmic membrane for the efficient capture of ferric hydroxamates; and FhuD1, a protein with similarity to FhuD2. Gene duplication likely gave rise to fhuD1 and fhuD2. While the genomic locations of fhuCBG and fhuD2 in S. aureus strains are conserved, both the presence and the location of fhuD1 are variable. The apparent redundancy of FhuD1 led us to examine the role of this protein. We demonstrate that FhuD1 is expressed only under conditions of iron limitation through the regulatory activity of Fur. FhuD1 fractions with the cell membrane and binds hydroxamate siderophores but with lower affinity than FhuD2. Using small angle x-ray scattering, the solution structure of FhuD1 resembles that of FhuD2, and only a small conformational change is associated with ferrichrome binding. FhuD1, therefore, appears to be a receptor for ferric hydroxamates, like FhuD2. Our data to date suggest, however, that FhuD1 is redundant to FhuD2 and plays a minor role in hydroxamate transport. However, given the very real possibility that we have not yet identified the proper conditions where FhuD1 does provide an advantage over FhuD2, we anticipate that FhuD1 serves an enhanced role in the transport of untested hydroxamate siderophores and that it may play a prominent role during the growth of S. aureus in its natural environments.

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“…In Gram negative bacteria, the cell possesses outer membrane complex receptors that supply the energy required for iron transport (Ton complex) which allow the iron to pass through the outer membrane and is internalized into the cytoplasm via the cell membrane. In Gram positive bacteria, the iron binding to lipoproteins anchored in the cytoplasmic membrane, thus must traverse this membrane and peptidoglycan [29] . Therefore doping with iron nanoparticles appears not to be a favorable option, at least when used as an antibacterial agent.…”

Section: Discussionmentioning

confidence: 99%

Antibacterial Activities of Nanoparticles of Titanium dioxide, Intrinsic and Doped With Indium and Iron

Amabye¹,

Internationals²

2016

JMCT

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The need for new antimicrobial compounds has been attention on developing new and emerging materials based on nanoparticles with antimicrobial activity. The aim of this research was to evaluate the antibacterial activities of nanoparticles of titanium dioxide, intrinsic and doped with Indium and Iron in Escherichia coli and Staphylococcus aureus. The bacteriostatic effect of TiO 2 nanoparticles (two samples), TiO 2 :Fe and TiO 2 :In with concentrations of 50, 250 500 µg/ml. It was observed by optical density measurements. The bactericidal effect was determined by plate count agar Muller-Hinton, where they were incubated for 12 hours: 50 µl of bacterial suspension (concentration 1.5 x 10 6 bacteria/ml), concentration 50 µl of nanoparticles suspended at concentrations between 39 and 2500 µg/ ml. Then, to 10 -6 dilutions were made and plated on agar for colony counts. There were significant decreases P < 0.05 in the bacterial optical densities with respect to control, using TiO 2 nanoparticles prepared with different contents of acetic acid at concentrations of 250 and 500 µg/ml versus E. coli and S. aureus. In the plate counts, there was a significant reduction, P < 0.05 in the number of CFU of E. coli using TiO 2 nanoparticles (50% AcAc) in concentrations 39 to 2500 µg/ml; in the case of S. aureus decrease seen in concentrations 78 to 2500 µg/ml. In both bacteria, we observed decreased bacterial growth with TiO 2 nanoparticles at concentrations of 156 -2500 µg/ml. The two variants of preparing TiO 2 nanoparticles have higher intrinsic activity against E. coli and S. aureus, while nanoparticles doped with Indium and Iron, not power the antibacterial effect.

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ABC transporter-mediated uptake of iron, siderophores, heme and vitamin B12

Cited by 238 publications

References 28 publications

Comparative Genomics of the Vitamin B12 Metabolism and Regulation in Prokaryotes

Comparative Genomics of the Vitamin B12 Metabolism and Regulation in Prokaryotes

FhuD1, a Ferric Hydroxamate-binding Lipoprotein in Staphylococcus aureus

Antibacterial Activities of Nanoparticles of Titanium dioxide, Intrinsic and Doped With Indium and Iron

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