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A more recent version of this article appeared on February 28, 2003
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M211729200v1
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Papers In Press, published online ahead of print December 19, 2002
J. Biol. Chem, 10.1074/jbc.M211729200
Submitted on November 18, 2002
Revised on December 19, 2002
Accepted on December 19, 2002

A novel protein tightly bound to bacterial magnetic particles in Magnetospirillum magneticum strain AMB-1

Atsushi Arakaki, John Webb, and Tadashi Matsunaga

Department of Biotechnology, Tokyo University of Agriculture and Technology, Koganei, Tokyo 184-8588

Corresponding Author: tmatsuna{at}cc.tuat.ac.jp

Magnetic bacteria synthesize magnetite crystals with species-dependent morphologies. The molecular mechanisms that control nano-magnetite crystal formation and the generation of diverse morphologies are not well understood. From the analysis of magnetite crystal associated proteins, several low molecular weight 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.


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