Identification of four new prokaryotic bacterioferritins, from Helicobacter pylori, Anabaena variabilis, Bacillus subtilis and Treponema pallidum, by analysis of gene sequences

Evans, Doyle J.; Evans, Dolores G.; Lampert, Heather C.; Nakano, Hironobu

doi:10.1016/0378-1119(94)00774-m

Cited by 80 publications

(70 citation statements)

References 26 publications

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“…The molecular mass of the deduced Dps was 17,332 Da, similar to the estimates from denaturing PAGE (data not shown). The primary structure of C. jejuni Dps has a high similarity to those of HP-NAP (16,43), E. coli Dps (4), and other members of the Dps family (6,11,13,35,51). family of proteins rather than to the ferritin or bacterioferritin group (Fig.…”

Section: Resultsmentioning

confidence: 99%

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

Ishikawa¹,

Mizunoe²,

et al. 2003

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whereas it did not appear to bind DNA. An isogenic dps-deficient mutant was more vulnerable to hydrogen peroxide than its parental strain, as judged by growth inhibition tests. The iron chelator Desferal restored the resistance of the Dps-deficient mutant to hydrogen peroxide, suggesting that this iron-binding protein prevented generation of hydroxyl radicals via the Fenton reaction. Dps was constitutively expressed during both exponential and stationary phase, and no induction was observed when the cells were exposed to H 2 O 2 or grown under iron-supplemented or iron-restricted conditions. On the basis of these data, we propose that this iron-binding protein in C. jejuni plays an important role in protection against hydrogen peroxide stress by sequestering intracellular free iron and is expressed constitutively to cope with the harmful effect of hydrogen peroxide stress on this microaerophilic organism without delay.

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Section: Resultsmentioning

confidence: 99%

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

Ishikawa¹,

Mizunoe²,

et al. 2003

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“…NEUTROPHIL-ACTI-VATING PROTEIN A. Neutrophil-activating protein A (NapA) is a dodecameric bacterioferritin comprising 12 identical 15-kDa subunits (34). As its name suggests, the primary role of NapA was originally thought to be neutrophil stimulation, by promoting neutrophil adhesion to endothelial cells and stimulating NADPH oxidase activity (35).…”

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Helicobacter pyloridefense against oxidative attack

Stent

Every

Sutton

2012

American Journal of Physiology-Gastrointestinal and Liver Physi

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“…An additional sequence of spa18 was obtained by methods reported previously by Evans et al (19). The 336-bp PCR product obtained above was purified, biotinylated, and then bound to streptavidin-coated magnetic beads.…”

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confidence: 99%

“…The 336-bp PCR product obtained above was purified, biotinylated, and then bound to streptavidin-coated magnetic beads. Chromosomal DNA from type 18 streptococci was partially digested with Sau3A and then ligated to synthetic oligonucleotide pairs (19) containing each half of the Sau3A sequence. The ligation mixture and bound PCR target were melted and mixed to capture spa-containing chromosomal sequences.…”

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confidence: 99%