• Author: Uebe, René

    Ludwig Maximillian University Munich, Department Biology I

  • Author: Junge, Katja

    Ludwig Maximillian University Munich, Department Biology I

  • Author: Henn, Verena

    Ludwig Maximillian University Munich, Department Biology I

  • Author: Poxleitner, Gabriele

    Ludwig Maximillian University Munich, Department Biology I

  • Author: Katzmann, Emanuel

    Ludwig Maximillian University Munich, Department Biology I

  • Author: Plitzko, Jürgen M.

    Max Planck Institute of Biochemistry, Department of Molecular Structural Biology

  • Author: Zarivach, Raz

    Ben Gurion University of the Negev, Department of Life Sciences and the National Institute of Biotechnology

  • Author: Kasama, Takeshi

    Center for Electron Nanoscopy, Technical University of Denmark, Fysikvej, 2800, Kongens Lyngby, Denmark

  • Author: Wanner, Gerhard

    Ludwig Maximillian University Munich, Department Biology I

  • Author: Pósfai, Mihály

    University of Pannonia, Department of Earth and Environmental Sciences

  • Author: Böttger, Lars

    University of Lübeck, Isotopes Laboratory

  • Author: Matzanke, Berthold

    University of Lübeck, Isotopes Laboratory

  • Author: Schüler, Dirk

    Ludwig Maximillian University Munich, Department Biology I

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Magnetotactic bacteria form chains of intracellular membrane‐enclosed, nanometre‐sized magnetite crystals for navigation along the earth's magnetic field. The assembly of these prokaryotic organelles requires several specific polypeptides. Among the most abundant proteins associated with the magnetosome membrane of Magnetospirillum gryphiswaldense are MamB and MamM, which were implicated in magnetosomal iron transport because of their similarity to the cation diffusion facilitator family. Here we demonstrate that MamB and MamM are multifunctional proteins involved in several steps of magnetosome formation. Whereas both proteins were essential for magnetite biomineralization, only deletion of mamB resulted in loss of magnetosome membrane vesicles. MamB stability depended on the presence of MamM by formation of a heterodimer complex. In addition, MamB was found to interact with several other proteins including the PDZ1 domain of MamE. Whereas any genetic modification of MamB resulted in loss of function, site‐specific mutagenesis within MamM lead to increased formation of polycrystalline magnetite particles. A single amino acid substitution within MamM resulted in crystals consisting of haematite, which coexisted with magnetite crystals. Together our data indicate that MamM and MamB have complex functions, and are involved in the control of different key steps of magnetosome formation, which are linked by their direct interaction.
Original languageEnglish
JournalMolecular Microbiology
Publication date2011
Volume82
Issue4
Pages818-835
ISSN0950-382X
DOIs
StatePublished
CitationsWeb of Science® Times Cited: 30
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