title: A novel protein tightly bound to bacterial magnetic particles in Magnetospirillum magneticum strain AMB-1.
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 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.
authors.affiliation: Department of Biotechnology, Tokyo University of Agriculture and Technology, Koganei, Japan.
authors.forename: Atsushi
authors.initials: A
authors.lastname: Arakaki
authors.forename: John
authors.initials: J
authors.lastname: Webb
authors.forename: Tadashi
authors.initials: T
authors.lastname: Matsunaga
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D001483:Base Sequence; D017931:DNA Primers; D008280:Magnetics; D008854:Microscopy, Electron; D008969:Molecular Sequence Data; D020560:Proteobacteria / Q000378:metabolism* / Q000648:ultrastructure
chemical_list: D001426:Bacterial Proteins; D017931:DNA Primers