The Iron-Binding Protein Dps Confers Hydrogen Peroxide Stress Resistance to
 Campylobacter jejuni

Ishikawa, Takahiro; Mizunoe, Yoshimitsu; Kawabata, Shun Ichiro; Takade, Akemi; Harada, Mine; Wai, Sun Nyunt; Yoshida, Shin Ichi

doi:10.1128/jb.185.3.1010-1017.2003

Cited by 122 publications

(116 citation statements)

References 58 publications

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“…Both halves were then stained with the Ferene-S stain described by Chung (Chung, 1985) and Ishikawa et al (Ishikawa et al, 2003). This consists of 1·mmol·l…”

Section: Demonstration Of Iron Binding: Electrophoresis and Blottingmentioning

confidence: 99%

The role of metals in molluscan adhesive gels

Werneke

Swann

Farquharson

et al. 2007

Journal of Experimental Biology

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SUMMARY Several gastropod molluscs produce glues that are interesting because they are dilute gels and yet they produce strong adhesion. Specific glue proteins have been identified that play a central role in this adhesion, possibly by crosslinking other polymers in the gel. This study investigates the role of metals in the action of these glue proteins. Atomic absorption spectrometry showed that glue from the slug Arion subfuscus contains substantial quantities of zinc (46±7 p.p.m. and 189±80 p.p.m. in two different sets of experiments) and also iron, copper and manganese (2–7 p.p.m.). Iron-specific staining demonstrates that iron is bound specifically to the 15 kDa glue protein. Several approaches were used to show that these metals have important functional effects. Adding iron or copper to dissolved glue causes the proteins to precipitate rapidly, although zinc has no effect. Removing iron and related transition metals with a chelator during secretion of the glue causes a sixfold increase in the solubility of the glue. Once the glue has set, however, removing these metals has no effect. Finally, the gel-stiffening activity of the glue proteins was measured in the presence and absence of the chelator. The chelator eliminated the gel-stiffening effect of the proteins, suggesting that transition metals were necessary for the proteins to act on the gel. Thus, the glue contains transition metals and these metals play an essential role in glue function.

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“…Both halves were then stained with the Ferene-S stain described by Chung (Chung, 1985) and Ishikawa et al (Ishikawa et al, 2003). This consists of 1·mmol·l…”

Section: Demonstration Of Iron Binding: Electrophoresis and Blottingmentioning

confidence: 99%

The role of metals in molluscan adhesive gels

Werneke

Swann

Farquharson

et al. 2007

Journal of Experimental Biology

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“…H 2 O 2 ) (17)(18)(19)(20), nutrient starvation (13,15,21), and the presence of ethanol (15,16). Although Dps proteins are not essential for cell viability under normal growth conditions, it was shown that Dps deletion mutants of some bacteria are susceptible to oxidative stress (22)(23)(24), acids, bases, or UV radiation (25). Dps proteins can be induced by increasing iron concentrations in the medium (18) and may be up-regulated during iron starvation (19,26).…”

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confidence: 99%

Structure and Mechanism of Iron Translocation by a Dps Protein from Microbacterium arborescens

Pesek

Büchler

Albrecht

et al. 2011

Journal of Biological Chemistry

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Dps (DNA protection during starvation) enzymes are a major class of dodecameric proteins that bacteria use to detoxify their cytosol through the uptake of reactive iron species. In the stationary growth phase of bacteria, Dps enzymes are primarily used to protect DNA by biocrystallization. To characterize the wild type Dps protein from Microbacterium arborescens that displays additional catalytic functions (amide hydrolysis and synthesis), we determined the crystal structure to a resolution of 2.05 Å at low iron content. The structure shows a single iron at the ferroxidase center coordinated by an oxo atom, one water molecule, and three ligating residues. An iron-enriched protein structure was obtained at 2 Å and shows the stepwise uptake of two hexahydrated iron atoms moving along channels at the 3-fold axis before a restriction site inside the channels requires removal of the hydration sphere. Supporting biochemical data provide insight into the regulation of this acylamino acid hydrolase. Moreover, the peroxidase activity of the protein was determined. The influence of iron and siderophores on the expression of acylamino acid hydrolase was monitored during several stages of cell growth. Altogether our data provide an interesting view of an unusual Dps-like enzyme evolutionarily located apart from the large Dps sequence clusters.Iron is an essential element for cells as the cofactor in numerous enzymes. The element plays a fundamental role in cell respiration, for example as a component of cytochromes and iron-sulfur proteins. In addition, many processes such as photosynthesis, nitrogen fixation, and methanogenesis are strictly iron-dependent (1). Remarkably, iron of the two redox states differs in solubility: the reduced ferrous Fe 2ϩ form is soluble at 10 Ϫ1 M, whereas the oxidized ferric Fe 3ϩ species is highly insoluble at physiological pH.Bacteria regulate iron homeostasis using iron-sensing repressors such as Fur in Escherichia coli (1-3). Fur mainly regulates the synthesis and transport of siderophores, low molecular weight compounds with a high affinity for Fe 3ϩ that are secreted into the external medium (1). The poor bioavailability of iron often limits bacterial growth (1 Bacteria are protected against H 2 O 2 and ROS by different enzymes such as superoxide dismutases, superoxide reductases, catalases, and Dps proteins (DNA protection during starvation) (4). Dps proteins belong to the superfamily of the ferritin fold but, unlike the 24-mer ferritins, in prokaryotes they occur only as 12-meric complexes with a slightly variable architecture (5). They are active in Fe 2ϩ uptake, oxidation, storage, and H 2 O 2 destruction (1, 6, 7) and also provide physical protection by binding DNA and forming ordered material as shown for E. coli (8, 9), Bacillus cereus (10), and the marine cyanobacterium Trichodesmium erythraeum (11

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“…The presence of Dps homologs in a wide variety of microorganisms, though with molecular divergence, suggests their importance for microorganisms' survival under many kinds of stressful environments. In most organisms Dps serves as an iron-binding protein and protects the organism from oxygen stresses (7,8,10,15). In addition, Halsey et al reported the contribution of dps to Salmonella stress resistance, survival in macrophages, and virulence in mice (7).…”

Section: Discussionmentioning

confidence: 99%

Expression and Degradation of SEp22, a Pathogenicity-Related Protein of Salmonella Dps, in Salmonella enterica serovar Enteritidis Isolated from the Poultry Farms in Japan

Terai

Yamasaki²,

Igimi³

et al. 2005

Bioscience Microflora

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We isolated and characterized a pathogenicity-related protein in Salmonella enterica serovar Enteritidis (SE) from poultry farms, and designated it as SEp22, which has recently been identified with Salmonella Dps, a DNA-binding protein (12, 13, Amano et al., manuscript in preparation). Expression of SEp22 was shown to be transcriptionally regulated, because another SE strain without virulence was found to possess a full-length non-mutated gene of sep22, but had little expression of SEp22 mRNA and much lower levels of SEp22 protein compared to the virulent standard strain SE Cl#15-1. Besides, expression of SEp22 was connected with bacterial growth, showing reduced expression in the logarithmic phase but increased expression from the late logarithmic to stationary phases. These changes were slightly later than those in σ 38 levels as well as SEp22 mRNA, suggesting that expression of SEp22 is under transcriptional control through RNA polymerase activity by σ 38 . In addition, high levels of SEp22 in the stationary phase were rapidly reduced upon incubation of the bacteria in fresh medium. This reduction was dependent on bacterial concentration in the culture, temperature, and time of incubation, suggesting proteolytic degradation of SEp22 in growing bacteria.

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The Iron-Binding Protein Dps Confers Hydrogen Peroxide Stress Resistance to Campylobacter jejuni

Cited by 122 publications

References 58 publications

The role of metals in molluscan adhesive gels

The role of metals in molluscan adhesive gels

Structure and Mechanism of Iron Translocation by a Dps Protein from Microbacterium arborescens

Expression and Degradation of SEp22, a Pathogenicity-Related Protein of <i>Salmonella</i> Dps, in <i>Salmonella enterica</i> serovar Enteritidis Isolated from the Poultry Farms in Japan

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