Structural heterogeneity of Pseudomonas aeruginosa bacterioferritin

Moore, Geoffrey R.; Kadir, Fahmi H.A.; al-Massad, F K; Brun, Nick E. Le; Thomson, Andrew J.; Greenwood, C. T.; Keen, Jeffrey N.; Findlay, John B. C.

doi:10.1042/bj3040493

Cited by 40 publications

(34 citation statements)

References 31 publications

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“…Met52--+Thr52 is reported for Pseudomonas aeruginosa (a) (Moore et aL, 1994) and Cyanobacterium synechocystis (Laulh~re, Laboure, van Wuytswinkel & Gagnon, 1992) (Fig. 3).…”

Section: The Haem Binding Sitementioning

confidence: 73%

“…Asp50 and Asp126 are often conserved in bacterioferritin sequences but can be replaced by Glu in P. aeruginosa (a) (Moore et al, 1994), Nitrobacter winogradskyi (Kurokawa, Fukumori & Yamanaka, 1989), Rhodobacter capsulatus (Penfold, Ringeling, Moore, McEwan & Spiro, 1996) and Brucella melitensis (Denoel et al, 1995), or by Ser in Azotobacter vinelandii (Grossman, Hinton, Minak-Bernero, Slaughter & Stiefel, 1992).…”

Section: Discussionmentioning

confidence: 99%

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Structure of a Monoclinic Crystal Form of Cytochrome b1 (Bacterioferritin) from E. coli

Dautant

Meyer

Yariv

et al. 1998

Acta Crystallogr D Biol Crystallogr

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Crystals of E. coli cytochrome b l, alias bacterioferritin, were grown from a low ionic strength solution. The resulting monoclinic P21 structure was solved by molecular replacement and refined using noncrystallographic symmetries applied to the fundamental unit, consisting of two protein subunits and a single haem. From the Patterson self-rotation results it was shown that the asymmetric unit of the monoclinic crystal consists of 12 such dimers and corresponds to a complete, nearly spherical, molecule of bacterioferritin (Mr = 450 kDa) of 432 point-group symmetry. It is thus the most symmetrical cytochrome. As previously determined for the tetragonal form, the haem is located in a special position on a local twofold axis of the dimer. A bimetal centre is also observed within the four-helix bundle of each monomer; a metal-binding site is located on the fourfold axis. discovery in

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“…Met52--+Thr52 is reported for Pseudomonas aeruginosa (a) (Moore et aL, 1994) and Cyanobacterium synechocystis (Laulh~re, Laboure, van Wuytswinkel & Gagnon, 1992) (Fig. 3).…”

Section: The Haem Binding Sitementioning

confidence: 73%

Section: Discussionmentioning

confidence: 99%

Structure of a Monoclinic Crystal Form of Cytochrome b1 (Bacterioferritin) from E. coli

Dautant

Meyer

Yariv

et al. 1998

Acta Crystallogr D Biol Crystallogr

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“…Pea seed ferritin also gives two bands, the smaller of which is again thought to arise from the larger by a specific cleavage promoted by hydroxyl radicals. However, subunit sequence heterogeneity has recently been reported for the Bfr from Pseudomonas aeruginosa [24]. In the fungus A. spinosa the N-terminal amino acid sequences of the upper and lower mycelial band shown in Fig.…”

Section: Resultsmentioning

confidence: 99%

“…When the N-terminal sequences reported here for the two subunits of mycelial ferritin from A. spinosa were checked against the sequences in the National Center for Biotechnology Information (NCBI-NLM) component data banks, all of the high scoring matches were bacterioferritins. The degree of homology of the lower band ranged from 44% identity with mycobacterial Bfr and Bfr from A. winograskyi to 80% identity between it and the c~-subunit of Bfr from Pseudomonas aeruginosa [24]. Interestingly, the latter two Bfrs exhibit sequences of 20 amino acids stretching from Gly-17 to Gly-36 which are, except for one difference (Leu-26/Phe), identical.…”

Section: Resultsmentioning

confidence: 99%

Fungal ferritins: The ferritin from mycelia of Absidia spinosa is a bacterioferritin

Carrano¹,

Böhnke²,

Matzanke³

1996

FEBS Letters

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Two distinct ferritin like iron containing proteins have been identified and isolated from the fungus Absidia spinosa; one from the spores and another from the mycelia. The mycelial protein has been purified and consists of two subunits of approx. 20 kDa. The N-terminal sequences of both subunits have been determined. The holoprotein as isolated contains approx. 750 iron atoms/molecule and exhibits a beme-like UV-Vis spectrum. Based on the beme spectrum and the high degree of sequence homology found, it has been established that the mycelial protein is a bacterioferritin. This is the first example demonstrating the presence of a bacterioferritin in a eukaryotic organism.

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“…BfrA, composed of 24 subunits and capable of binding 700 iron atoms, is the major iron storage protein in P. aeruginosa (31). The results of Ma et al (30) suggest that BfrA is required as a source of iron for the heme prothetic group of KatA.…”

Section: Monitoring Kata and Ahpc Proteins In H Pylori Cell Extract mentioning

confidence: 99%

Role of a Bacterial Organic Hydroperoxide Detoxification System in Preventing Catalase Inactivation

Wang¹,

Conover

Benoit³

et al. 2004

Journal of Biological Chemistry

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In the gastric pathogen Helicobacter pylori, catalase (KatA) and alkyl hydroperoxide reductase (AhpC) are two highly abundant enzymes that are crucial for oxidative stress resistance and survival of the bacterium in the host. Here we report a connection unidentified previously between the two stress resistance enzymes. We observed that the catalase in ahpC mutant cells in comparison with the parent strain is inactivated partially (approximately 50%). The decrease of catalase activity is well correlated with the perturbation of the heme environment in catalase, as detected by electron paramagnetic resonance spectroscopy. To understand the reason for this catalase inactivation, we examined the inhibitory effects of hydroperoxides on H. pylori catalase (either present in cell extracts or added to the purified enzyme) by monitoring the enzyme activity and the EPR signal of catalase. H. pylori catalase is highly resistant to its own substrate, without the loss of enzyme activity by treatment with a molar ratio of 1:3000 H 2 O 2 . However, it is inactivated by lower concentrations of organic hydroperoxides (the substrate of AhpC). Treatment with a molar ratio of 1:400 t-butyl hydroperoxide resulted in an inactivation of catalase by approximately 50%. UV-visible absorption spectra indicated that the catalase inactivation by organic hydroperoxides is caused by the formation of a catalytically incompetent compound II species. To further support the idea that organic hydroperoxides, which accumulate in the ahpC mutant cells, are responsible for the inactivation of catalase, we compared the level of lipid peroxidation found in ahpC mutant cells with that found in wild type cells. The results showed that the total amount of extractable lipid hydroperoxides in the ahpC mutant cells is approximately three times that in the wild type cells. Our findings reveal a novel role of the organic hydroperoxide detoxification system in preventing catalase inactivation.

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Structural heterogeneity of Pseudomonas aeruginosa bacterioferritin

Cited by 40 publications

References 31 publications

Structure of a Monoclinic Crystal Form of Cytochrome b1 (Bacterioferritin) from E. coli

Structure of a Monoclinic Crystal Form of Cytochrome b1 (Bacterioferritin) from E. coli

Fungal ferritins: The ferritin from mycelia of Absidia spinosa is a bacterioferritin

Role of a Bacterial Organic Hydroperoxide Detoxification System in Preventing Catalase Inactivation

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