NreB from
            <i>Achromobacter xylosoxidans</i>
            31A Is a Nickel-Induced Transporter Conferring Nickel Resistance

Grass, Gregor; Fan, Baochao; Rosen, Barry P.; Lemke, Karen; Schlegel, Hans-Günter; Rensing, Christopher

doi:10.1128/jb.183.9.2803-2807.2001

Cited by 90 publications

(55 citation statements)

References 26 publications

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“…The protein concentration of purified CueO was determined at 280 nm (ε CueO ϭ 63063 M Ϫ1 cm Ϫ1 ). The ␤-galactosidase activity in permeabilized cells was determined as published previously (11,20).…”

Section: Methodsmentioning

confidence: 99%

Linkage between Catecholate Siderophores and the Multicopper Oxidase CueO in Escherichia coli

et al. 2004

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The multicopper oxidase CueO had previously been demonstrated to exhibit phenoloxidase activity and was implicated in intrinsic copper resistance in Escherichia coli. Catecholates can potentially reduce Cu(II) to the prooxidant Cu(I). In this report we provide evidence that CueO protects E. coli cells by oxidizing enterobactin, the catechol iron siderophore of E. coli, in the presence of copper. In vitro, a mixture of enterobactin and copper was toxic for E. coli cells, but the addition of purified CueO led to their survival. Deletion of fur resulted in copper hypersensitivity that was alleviated by additional deletion of entC, preventing synthesis of enterobactin. In addition, copper added together with 2,3-dihydroxybenzoic acid or enterobactin was able to induce a ⌽(cueO-lacZ) operon fusion more efficiently than copper alone. The reaction product of the 2,3-dihydroxybenzoic acid oxidation by CueO that can complex Cu(II) ions was determined by gas chromatography-mass spectroscopy and identified as 2-carboxymuconate.

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Section: Methodsmentioning

confidence: 99%

Linkage between Catecholate Siderophores and the Multicopper Oxidase CueO in Escherichia coli

et al. 2004

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“…strain PCC 6803 (6) and NreB from R. metallidurans (7). Indeed, all are membrane-bound proteins which possess a histidine-rich domain.…”

Section: (ϯ2) Nmol Of Paranitrophenol (Pnp) ⅐ Minmentioning

confidence: 99%

“…There is no evidence for the transport of nickel by one of these two modes of efflux. Instead, this metal can be transported outside the cytoplasm by NreB from R. metallidurans (7) or NrsD from Synechocystis sp. strain PCC 6803 (6), which are members of the major facilitator superfamily and which each exhibit 12 putative transmembrane helices and a histidine-rich carboxy terminus contributing to nickel resistance.…”

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confidence: 99%

Identification of rcnA ( yohM ), a Nickel and Cobalt Resistance Gene in Escherichia coli

2005

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We report here on the isolation and primary characterization of the yohM gene of Escherichia coli. We show that yohM encodes a membrane-bound polypeptide conferring increased nickel and cobalt resistance in E. coli. yohM was specifically induced by nickel or cobalt but not by cadmium, zinc, or copper. Mutation of yohM increased the accumulation of nickel inside the cell, whereas cells harboring yohM in multicopy displayed reduced intracellular nickel content. Our data support the hypothesis that YohM is the first described efflux system for nickel and cobalt in E. coli. We propose rcnA (resistance to cobalt and nickel) as the new denomination of yohM.Nickel and cobalt are both required as trace elements in prokaryotes to fulfill a variety of metabolic functions, but high intracellular concentrations of these transition metals are toxic. One of the strategies evolved by bacteria to prevent damage is to export excess metal by efflux systems. Plasmid-borne determinants responsible for nickel and/or cobalt resistance have been described for the heavy-metal-resistant bacterium Ralstonia metallidurans (11,15), among which are members of the resistance-nodulation-cell division superfamily: the best-characterized CzcCBA (cobalt-zinc-cadmium) three-component cation antiporter (14) and the homologous CnrCBA (cobaltnickel resistance) (10) and NccCBA (nickel-cobalt-cadmium resistance) (18) efflux systems. Moreover, cobalt can be extruded from the cytoplasm by the cation diffusion facilitator CzcD of R. metallidurans at the expense of the proton motive force or a potassium gradient (15). Cobalt may also be a substrate of Zn-CPx-type ATPases, as in Helicobacter pylori (8). There is no evidence for the transport of nickel by one of these two modes of efflux. Instead, this metal can be transported outside the cytoplasm by NreB from R. metallidurans (7) or NrsD from Synechocystis sp. strain PCC 6803 (6), which are members of the major facilitator superfamily and which each exhibit 12 putative transmembrane helices and a histidine-rich carboxy terminus contributing to nickel resistance.In Escherichia coli, anaerobic hydrogenase isoenzymes and urease (in ureolytic strains) require incorporation of nickel to become active (12). Complex assembly processes involve accessory proteins, namely, HypB, implicated in nickel insertion into hydrogenase, and UreE, which delivers nickel to urease. HypB and UreE are well conserved among bacteria apart from a terminal histidine-rich stretch whose function would be nickel storage and which is absent in E. coli proteins (3, 5). In order to gain insights into nickel trafficking and, more precisely, to find proteins that would be involved in nickel resistance, we searched the E. coli genome database with a query based on a consensus alignment of the UreE and HypB histidine-rich variants. The best returned hit was yohM, whose product bears a histidine-rich domain in its center. The aim of the present work is to demonstrate the implication of yohM in nickel and cobalt trafficking in E. coli.Inactivati...

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“…Its properties allow it to bind both DNA and proteins and disrupt many cellular functions when present in excess (3). Several bacterial nickel efflux systems have been described that confer resistance to high levels of the metal (4,5). At the same time, nickel is known to be an essential cofactor in several bacterial enzymes (6) and is essential for anaerobic metabolism (7), so the cell must be able both to import and export nickel to maintain an appropriate non-toxic concentration in the cytoplasm.…”

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confidence: 99%

Crystal Structures of the Liganded and Unliganded Nickel-binding Protein NikA from Escherichia coli

Heddle

Scott

Unzai

et al. 2003

Journal of Biological Chemistry

114

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Bacteria have evolved a number of tightly controlled import and export systems to maintain intracellular levels of the essential but potentially toxic metal nickel. Nickel homeostasis systems include the dedicated nickel uptake system nik found in Escherichia coli, a member of the ABC family of transporters, that involves a periplasmic nickel-binding protein, NikA. This is the initial nickel receptor and mediator of the chemotactic response away from nickel. We have solved the crystal structure of NikA protein in the presence and absence of nickel, showing that it behaves as a "classical" periplasmic binding protein. In contrast to other binding proteins, however, the ligand remains accessible to the solvent and is not completely enclosed. No direct bonds are formed between the metal cation and the protein. The nickel binding site is apolar, quite unlike any previously characterized protein nickel binding site. Despite relatively weak binding, NikA is specific for nickel. Using isothermal titration calorimetry, the dissociation constant for nickel was found to be ϳ10 M and that for cobalt was approximately 20 times higher.

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NreB from Achromobacter xylosoxidans 31A Is a Nickel-Induced Transporter Conferring Nickel Resistance

Cited by 90 publications

References 26 publications

Linkage between Catecholate Siderophores and the Multicopper Oxidase CueO in Escherichia coli

Linkage between Catecholate Siderophores and the Multicopper Oxidase CueO in Escherichia coli

Identification of rcnA ( yohM ), a Nickel and Cobalt Resistance Gene in Escherichia coli

Crystal Structures of the Liganded and Unliganded Nickel-binding Protein NikA from Escherichia coli

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