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

Manuela Bozzi, Giuseppina Mignogna, Simonetta Stefanini, Donatella Barra, Catia Longhi, Piera Valenti, Emilia Chiancone
1997 Journal of Biological Chemistry  
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
more » ... ences 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.
doi:10.1074/jbc.272.6.3259 pmid:9013563 fatcat:bzrsc4pkivhahfga2vjmyyfelm