The FtsZ-Like Protein FtsZm of Magnetospirillum gryphiswaldense Likely Interacts with Its Generic Homolog and Is Required for Biomineralization under Nitrate Deprivation |
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| Authors: | Frank D. Müller Oliver Raschdorf Hila Nudelman Maxim Messerer Emanuel Katzmann Jürgen M. Plitzko Raz Zarivach Dirk Schüler |
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| Affiliation: | aLudwig Maximilian University Munich, Department Biology I, Biocenter, Planegg-Martinsried, Germany;bMax Planck Institute of Biochemistry, Department of Molecular Structural Biology, Planegg-Martinsried, Germany;cBijvoet Center for Biomolecular Research, Utrecht University, CH Utrecht, The Netherlands;dBen Gurion University of the Negev, Faculty of Natural Sciences, Department of Life Sciences, Beer-Sheva, Israel |
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| Abstract: | Midcell 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 FtsZ-dependent 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. |
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