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  The FtsZ-Like Protein FtsZm of Magnetospirillum gryphiswaldense Likely Interacts with Its Generic Homolog and Is Required for Biomineralization under Nitrate Deprivation

Müller, F. D., Raschdorf, O., Nudelman, H., Messerer, M., Katzmann, E., Plitzko, J. M., et al. (2014). The FtsZ-Like Protein FtsZm of Magnetospirillum gryphiswaldense Likely Interacts with Its Generic Homolog and Is Required for Biomineralization under Nitrate Deprivation. JOURNAL OF BACTERIOLOGY, 196(3), 650-659. doi:10.1128/JB.00804-13.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0019-0EE3-7 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0019-0EE6-1
Genre: Journal Article

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 Creators:
Müller, Frank D.1, Author
Raschdorf, Oliver2, Author              
Nudelman, Hila1, Author
Messerer, Maxim1, Author
Katzmann, Emanuel2, Author              
Plitzko, Jürgen M.2, Author              
Zarivach, Raz1, Author
Schüler, Dirk1, Author
Affiliations:
1external, ou_persistent22              
2Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565142              

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Free keywords: GREEN FLUORESCENT PROTEIN; CELL-DIVISION; MAGNETOTACTIC BACTERIA; ESCHERICHIA-COLI; MAGNETOSOME ISLAND; MAGNETITE BIOMINERALIZATION; SINORHIZOBIUM-MELILOTI; CHLOROPLAST FTSZ1; PLASTID DIVISION; RING STRUCTURE
 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 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.

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Language(s): eng - English
 Dates: 2014-02
 Publication Status: Published in print
 Pages: 10
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: ISI: 000332625000015
DOI: 10.1128/JB.00804-13
 Degree: -

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Title: JOURNAL OF BACTERIOLOGY
Source Genre: Journal
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Publ. Info: 1752 N ST NW, WASHINGTON, DC 20036-2904 USA : AMER SOC MICROBIOLOGY
Pages: - Volume / Issue: 196 (3) Sequence Number: - Start / End Page: 650 - 659 Identifier: ISSN: 0021-9193