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

Arakaki, A., Webb, J. and Matsunaga, T. (2003) A novel protein tightly bound to bacterial magnetic particles in Magnetospirillum magneticum strain AMB-1. Journal of Biological Chemistry, 278 (10). pp. 8745-8750.

Link to Published Version: http://dx.doi.org/10.1074/jbc.M211729200
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Abstract

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 magneticumstrain 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.

Publication Type: Journal Article
Murdoch Affiliation: School of Biological Sciences and Biotechnology
Publisher: American Society for Biochemistry and Molecular Biology Inc.
Copyright: © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
URI: http://researchrepository.murdoch.edu.au/id/eprint/16953
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