dMidcell selection, septum formation, and cytokinesis in most bacteria are orchestrated by the eukaryotic tubulin homolog FtsZ. The alphaproteobacterium Magnetospirillum gryphiswaldense (MSR-1) septates asymmetrically, and cytokinesis is linked to splitting and segregation of an intracellular chain of membrane-enveloped magnetite crystals (magnetosomes). In addition to a generic, full-length ftsZ gene, MSR-1 contains a truncated ftsZ homolog (ftsZm) which is located adjacent to genes controlling biomineralization and magnetosome chain formation. We analyzed the role of FtsZm in cell division and biomineralization together with the full-length MSR-1 FtsZ protein. Our results indicate that loss of FtsZm has a strong effect on microoxic magnetite biomineralization which, however, could be rescued by the presence of nitrate in the medium. Fluorescence microscopy revealed that FtsZm-mCherry does not colocalize with the magnetosome-related proteins MamC and MamK but is confined to asymmetric spots at midcell and at the cell pole, coinciding with the FtsZ protein position. In Escherichia coli, both FtsZ homologs form distinct structures but colocalize when coexpressed, suggesting an FtsZdependent recruitment of FtsZm. In vitro analyses indicate that FtsZm is able to interact with the FtsZ protein. Together, our data suggest that FtsZm shares key features with its full-length homolog but is involved in redox control for magnetite crystallization.
Magnetotactic bacteria (MTB) produce magnetosomes to navigate along Earth's magnetic field lines toward growth-favoring microoxic environments. Magnetosomes consist of nanometer-sized membrane-enveloped magnetite crystals and have recently emerged as a model system to study formation of prokaryotic organelles (1). In the alphaproteobacterium Magnetospirillum gryphiswaldense MSR-1 (in the following, referred to as MSR-1) and related magnetospirilla, the intracellular organelles are attached to a filamentous cytoskeletal structure formed by the actinlike MamK protein (2, 3, 4) which assembles magnetosomes into a cohesive chain (5). This magnetosome chain generates a magnetic moment which aligns the cell in external magnetic fields. In order to be cleaved evenly during cytokinesis and to be equipartitioned to daughter cells, the magnetosome chain is positioned at midcell. After cytokinesis, daughter chains are translocated to midcell again, suggesting that chain separation and relocalization are coordinated with the cell cycle.A crucial factor for midcell determination and septum formation in most bacteria is the conserved tubulin homolog FtsZ. FtsZ monomers assemble in a GTP-dependent manner to form protofilaments that align into higher-ordered structures by lateral selfinteraction assisted by accessory proteins. The FtsZ polymers are membrane tethered by C-terminal interaction with FtsA and build ring-or arc-like structures at future division sites (6). These FtsZ assemblies recruit further cell division proteins to finally build the divisome complex (7,8). Several factors have ...