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(Received for publication, October 15, 1996)
From the 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.
Volume 272, Number 6,
Issue of February 7, 1997
pp. 3259-3265
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
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