A Novel Non-heme Iron-binding Ferritin Related to the DNA-binding Proteins of the Dps Family in Listeria innocua

A multimeric protein that behaves functionally as an authentic ferritin has been isolated from the Gram-positive bacterium Listeria innocua The purified protein has a molecular mass of about 240,000 Da and is composed of a single type of subunit (18,000 Da). L. innocua ferritin is able to oxidize an...

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Bibliographic Details
Published in:The Journal of biological chemistry 1997-02, Vol.272 (6), p.3259-3265
Main Authors: Bozzi, Manuela, Mignogna, Giuseppina, Stefanini, Simonetta, Barra, Donatella, Longhi, Catia, Valenti, Piera, Chiancone, Emilia
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Bacterial Proteins - chemistry
Circular Dichroism
DNA-Binding Proteins - chemistry
Ferritins - chemistry
Listeria - chemistry
Listeria innocua
Molecular Sequence Data
Molecular Weight
Sequence Alignment
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Summary:A multimeric protein that behaves functionally as an authentic ferritin has been isolated from the Gram-positive bacterium Listeria innocua The purified protein has a molecular mass of about 240,000 Da and is composed of a single type of subunit (18,000 Da). L. innocua ferritin is able to oxidize and sequester about 500 iron atoms inside the protein cage. The primary structure reveals a high similarity to the DNA-binding proteins designated Dps. Among the proven ferritins, the most similar sequences are those of mammalian L chains that appear to share with L. innocua ferritin the negatively charged amino acids corresponding to the iron nucleation site. In L. innocua ferritin, an additional aspartyl residue may provide a strong complexing capacity that renders the iron oxidation and incorporation processes extremely efficient. This study provides the first experimental evidence for the existence of a non-heme bacterial ferritin that is related to Dps proteins, a finding that lends support to the recent suggestion of a common evolutionary origin of these two protein families.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.272.6.3259