The cation diffusion facilitator proteins MamB and MamM of Magnetospirillum gryphiswaldense have distinct and complex functions, and are involved in magnetite biomineralization and magnetosome membrane assembly

René Uebe, Katja Junge, Verena Henn, Gabriele Poxleitner, Emanuel Katzmann, Jürgen M. Plitzko, Raz Zarivach, Takeshi Kasama, Gerhard Wanner, Mihály Pósfai, Lars Böttger, Berthold Matzanke, Dirk Schüler

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    Abstract

    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
    Volume82
    Issue number4
    Pages (from-to)818-835
    ISSN0950-382X
    DOIs
    Publication statusPublished - 2011

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