4.5 Article

Co-ordinated functions of Mms proteins define the surface structure of cubo-octahedral magnetite crystals in magnetotactic bacteria

Journal

MOLECULAR MICROBIOLOGY
Volume 93, Issue 3, Pages 554-567

Publisher

WILEY
DOI: 10.1111/mmi.12683

Keywords

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Funding

  1. Japan Society for the Promotion of Science (JSPS) [23226016]
  2. Ministry of Education, Culture, Sports, Science and Technology, Japan (MEXT) [2206]
  3. Grants-in-Aid for Scientific Research [22107009, 23226016] Funding Source: KAKEN

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Magnetotactic bacteria synthesize magnetosomes comprised of membrane-enveloped single crystalline magnetite (Fe3O4). The size and morphology of the nano-sized magnetite crystals (< 100 nm) are highly regulated and bacterial species dependent. However, the control mechanisms of magnetite crystal morphology remain largely unknown. The group of proteins, called Mms (Mms5, Mms6, Mms7, and Mms13), was previously isolated from the surface of cubooctahedral magnetite crystals in Magnetospirillum magneticum strain AMB-1. Analysis of an mms6 gene deletion mutant suggested that the Mms6 protein plays a major role in the regulation of magnetite crystal size and morphology. In this study, we constructed various mms gene deletion mutants and characterized the magnetite crystals formed by the mutant strains. Comparative analysis showed that all mms genes were involved in the promotion of crystal growth in different manners. The phenotypic characterization of magnetites also suggested that these proteins are involved in controlling the geometries of the crystal surface structures. Thus, the co-ordinated functions of Mms proteins regulate the morphology of the cubo-octahedral magnetite crystals in magnetotactic bacteria.

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