The iron-binding protein Dps confers hydrogen peroxide stress resistance to Campylobacter jejuni

Takahiko Ishikawa, Yoshimitsu Mizunoe, Shun ichiro Kawabata, Akemi Takade, Mine Harada, Sun Nyunt Wai, Shin ichi Yoshida

研究成果: ジャーナルへの寄稿記事

86 引用 (Scopus)

抄録

We identified and characterized the iron-binding protein Dps from Campylobacter jejuni. Electron microscopic analysis of this protein revealed a spherical structure of 8.5 nm in diameter, with an electron-dense core similar to those of other proteins of the Dps (DNA-binding protein from starved cells) family. Cloning and sequencing of the Dps-encoding gene (dps) revealed that a 450-bp open reading frame (ORF) encoded a protein of 150 amino acids with a calculated molecular mass of 17,332 Da. Amino acid sequence comparison indicated a high similarity between C. jejuni Dps and other Dps family proteins. In C. jejuni Dps, there are iron-binding motifs, as reported in other Dps family proteins. C. jejuni Dps bound up to 40 atoms of iron per monomer, 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 H2O2 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.

元の言語英語
ページ(範囲)1010-1017
ページ数8
ジャーナルJournal of bacteriology
185
発行部数3
DOI
出版物ステータス出版済み - 2 1 2003

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Iron-Binding Proteins
Campylobacter jejuni
Hydrogen Peroxide
Iron
Proteins
Electrons
Deferoxamine
DNA-Binding Proteins
Chelating Agents
Protein C
Hydroxyl Radical
Open Reading Frames
Organism Cloning
Amino Acid Sequence
Amino Acids
DNA
Growth
Genes

All Science Journal Classification (ASJC) codes

  • Microbiology
  • Molecular Biology

これを引用

The iron-binding protein Dps confers hydrogen peroxide stress resistance to Campylobacter jejuni. / Ishikawa, Takahiko; Mizunoe, Yoshimitsu; Kawabata, Shun ichiro; Takade, Akemi; Harada, Mine; Wai, Sun Nyunt; Yoshida, Shin ichi.

:: Journal of bacteriology, 巻 185, 番号 3, 01.02.2003, p. 1010-1017.

研究成果: ジャーナルへの寄稿記事

Ishikawa, Takahiko ; Mizunoe, Yoshimitsu ; Kawabata, Shun ichiro ; Takade, Akemi ; Harada, Mine ; Wai, Sun Nyunt ; Yoshida, Shin ichi. / The iron-binding protein Dps confers hydrogen peroxide stress resistance to Campylobacter jejuni. :: Journal of bacteriology. 2003 ; 巻 185, 番号 3. pp. 1010-1017.
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abstract = "We identified and characterized the iron-binding protein Dps from Campylobacter jejuni. Electron microscopic analysis of this protein revealed a spherical structure of 8.5 nm in diameter, with an electron-dense core similar to those of other proteins of the Dps (DNA-binding protein from starved cells) family. Cloning and sequencing of the Dps-encoding gene (dps) revealed that a 450-bp open reading frame (ORF) encoded a protein of 150 amino acids with a calculated molecular mass of 17,332 Da. Amino acid sequence comparison indicated a high similarity between C. jejuni Dps and other Dps family proteins. In C. jejuni Dps, there are iron-binding motifs, as reported in other Dps family proteins. C. jejuni Dps bound up to 40 atoms of iron per monomer, 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 H2O2 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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