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J. Biol. Chem., Vol. 278, Issue 10, 8745-8750, March 7, 2003
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From the Magnetic bacteria synthesize magnetite crystals
with species-dependent morphologies. The molecular
mechanisms that control nano-sized magnetite crystal formation
and the generation of diverse morphologies are not well understood.
From the analysis of magnetite crystal-associated proteins,
several low molecular mass proteins tightly bound to bacterial
magnetite were obtained from Magnetospirillum magneticum
strain AMB-1. These proteins showed common features in their amino acid
sequences, which contain hydrophobic N-terminal and hydrophilic
C-terminal regions. The C-terminal regions in Mms5, Mms6, Mms7, and
Mms13 contain dense carboxyl and hydroxyl groups that bind iron ions.
Nano-sized magnetic particles similar to those in magnetic bacteria
were prepared by chemical synthesis of magnetite in the presence of the
acidic protein Mms6. These proteins may be directly involved in
biological magnetite crystal formation in magnetic bacteria.
The nucleotide sequence(s) reported in this paper has been submitted to the DDBJ/GenBankTM/EBI Data Bank with accession number(s) AB096081 and AB096082.
A Novel Protein Tightly Bound to Bacterial Magnetic
Particles in Magnetospirillum magneticum Strain
AMB-1*
,¶
Department of Biotechnology, Tokyo
University of Agriculture and Technology, Koganei, Tokyo 184-8588, Japan and the § Division of Science and Engineering, Murdoch
University, Perth, Western Australia 6150, Australia
*
This work was supported in part by Grant-in-aid for
Specially Promoted Research 13002005 from the Ministry of
Education, Culture, Sports, Science, and Technology of Japan and by a
visiting fellowship from the Japan Society for the Promotion of Science
(to J. W.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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