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

Atsushi Arakaki, John Webb, Tadashi Matsunaga

Research output: Contribution to journalArticle

274 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)8745-8750
Number of pages6
JournalJournal of Biological Chemistry
Volume278
Issue number10
DOIs
Publication statusPublished - 2003 Mar 7
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry

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