The Helicobacter pylori 19.6-kilodalton protein is an iron-containing protein resembling ferritin

Doig, P.; Austin, John W.; Trust, Trevor J.

doi:10.1128/jb.175.2.557-560.1993

Cited by 83 publications

(63 citation statements)

References 22 publications

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“…There exists some speculation that the roles of the mammalian and bacterio-type ferritins may in fact be somewhat different. This view is supported by the recent isolation of a mammalian-type ferritin from E. coli, an organism which also contains Bfr [13,14] as well as from Helicobacter pylori [15].…”

Section: Introductionmentioning

confidence: 93%

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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Section: Introductionmentioning

confidence: 93%

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

Carrano¹,

Böhnke²,

Matzanke³

1996

FEBS Letters

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“…Doig et al reported that approximately 20% of the total amount of ferritin-like protein was detected in membrane fraction and the majority of the protein was localized in the cytosolic fraction in Helicobacter pylori. 24) If the distribution of ferritin-like protein in MS-1 cell is similar to that observed in H. pylori, the Raman spectrum of …”

mentioning

confidence: 99%

Laser Raman Spectroscopic Study on Magnetite Formation in Magnetotactic Bacteria

et al. 2008

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Magnetotactic bacteria have one or more chains of magnetosome, consisting of nano-sized magnetic crystal covered with a phospholipid bilayer and use it to sense the geomagnetic fields. In order to elucidate the molecular process to make magnetosome from the iron compounds found in the bacteria, laser Raman spectroscopic measurements were performed with the magnetotactic bacterium, Magnetospirillum magnetotacticum MS-1 and the fractions separated from it. The major Raman signals at 662 cm À1 and 740 cm À1 were observed. The former was assigned to the Raman signal of magnetite and the latter, to that of ferrihydrite. The Raman signal of ferrihydrite was observed not only in the membrane fraction, but also in the cytoplasmic fraction. Based on the results, the role of ferrihydrite in magnetosome synthesis in the magnetotactic bacteria was discussed.

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“…However, it has been shown before that it is not advisable to draw conclusions from cellular fractionation studies alone. For example, Doig et al [21] observed 44% of the ferritin of H. pylori to be in the membrane fraction despite electron microscopy studies revealing it to be exclusively cytoplasmic [51]. Thus, additional data to support the fractionation studies are required.…”

Section: Conditionsmentioning

confidence: 97%

“…It is the presence of haem in purified Alternative bacterial iron-storage systems to bacterioferritin exist. Fenitin of the non-haem type, with a relatively high sequence similarity to animal fenitin, has been isolated from Helicobacter pylori [21] and Bacteroides fragilis [22], and its gene has been cloned from E. coli [23]. Furthermore, the 57Fe Mossbauer spectroscopy study of intact E. coli cells reported by Matzanke et al [24] clearly identified two ironrich species present in greater quantity than bacterioferritin that might constitute a novel iron-storage system.…”

mentioning

confidence: 99%

Iron metabolism in Rhodobacter capsulatus

Ringeling

Davy

Monkara

et al. 1994

European Journal of Biochemistry

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The water-soluble cytochrome b,,, from the photosynthetic bacterium Rhodobacter capsulatus was purified and shown to have the properties of the iron-storage protein bacterioferritin. The molecular mass of R. capsulatus bacterioferritin is 428 kDa and it is composed of a single type of 18-kDa subunit. The N-terminal amino acid sequence of the bacterioferritin subunit shows 70% identity to the sequence of bacterioferritin subunits from Escherichia coli, Nitrobacter winogradskyi, Azotobacter vinelandii and Synechocystis PCC 6803. The absorbance spectrum of reduced bacterioferritin shows absorbance maxima at 557 nm (a band), 526 nm @ band) and 417 nm (Soret band) from the six haem groups/molecule. Antibody assays reveal that bacterioferritin is located in the cytoplasm of R. capsulatus, and its levels stay relatively constant during batch growth under aerobic conditions when the iron concentration in the medium is kept constant. Iron deficiency leads to a decrease in bacterioferritin and iron overload leads to an increase. Bacterioferritin from R. capsulatus has an amorphous iron-oxide core with a high phosphate content (900-1000 Fe atoms and approximately 600 phosphateshacterioferritin molecule). Mossbauer spectroscopy indicates that in both aerobically and anaerobically (phototrophically) grown cells bacterioferritin with an Fe'+ core is formed, suggesting that iron-core formation in vivo may not always require molecular oxygen.Iron is an essential element for the growth of almost all bacteria and many of the molecular details of iron uptake have been established [l -51. The intracellular sequestration and mobilisation of iron have received little attention but a potential iron store which has been identified in Azotobacter vinelandii [6] [6,9, 101. N-terminal amino acid sequences of bacterioferritin polypeptides are highly similar [lo-141 and the molecular properties of these proteins indicate that they form a closely related family. Bacterioferritin, like its animal counterpart ferritin, is organised as a hollow protein shell which can contain a non-haem iron in its central cavity [6,[15][16][17]. Unlike mammalian ferritin, in which the non-haem iron core is crystalline ferrihydrite [16, 181, bacterioferritin has an amorphous iron core with a high phosphate content [19]. Another difference between mammalian fenitins and bacterioferritins is that the latter contain intrinsic haem groups while the former do not. It is the presence of haem in purified Alternative bacterial iron-storage systems to bacterioferritin exist. Fenitin of the non-haem type, with a relatively high sequence similarity to animal fenitin, has been isolated from Helicobacter pylori [21] and Bacteroides fragilis [22], and its gene has been cloned from E. coli [23]. Furthermore, the 57Fe Mossbauer spectroscopy study of intact E. coli cells reported by Matzanke et al. [24] clearly identified two ironrich species present in greater quantity than bacterioferritin that might constitute a novel iron-storage system.No iron-storage protein has been pr...

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The Helicobacter pylori 19.6-kilodalton protein is an iron-containing protein resembling ferritin

Cited by 83 publications

References 22 publications

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

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

Laser Raman Spectroscopic Study on Magnetite Formation in Magnetotactic Bacteria

Iron metabolism in Rhodobacter capsulatus

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