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  A gradient-forming MipZ protein mediating the control of cell division in the magnetotactic bacterium Magnetospirillum gryphiswaldense

Toro-Nahuelpan, M., Corrales-Guerrero, L., Zwiener, T., Osorio-Valeriano, M., Mueller, F.-D., Plitzko, J. M., et al. (2019). A gradient-forming MipZ protein mediating the control of cell division in the magnetotactic bacterium Magnetospirillum gryphiswaldense. MOLECULAR MICROBIOLOGY, 112(5), 1423-1439. doi:10.1111/mmi.14369.

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Toro-Nahuelpan, Mauricio1, Author              
Corrales-Guerrero, Laura2, Author
Zwiener, Theresa2, Author
Osorio-Valeriano, Manuel2, Author
Mueller, Frank-Dietrich2, Author
Plitzko, Jürgen M.1, Author              
Bramkamp, Marc2, Author
Thanbichler, Martin2, Author
Schueler, Dirk2, Author
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1Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565142              
2external, ou_persistent22              

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Free keywords: CHROMOSOME SEGREGATION; POLAR LOCALIZATION; BACILLUS-SUBTILIS; FTSZ; MAGNETOSOMES; SYSTEM; VISUALIZATION; INHIBITORBiochemistry & Molecular Biology; Microbiology;
 Abstract: Cell division needs to be tightly regulated and closely coordinated with other cellular processes to ensure the generation of fully viable offspring. Here, we investigate division site placement by the cell division regulator MipZ in the alphaproteobacterium Magnetospirillum gryphiswaldense, a species that forms linear chains of magnetosomes to navigate within the geomagnetic field. We show that M. gryphiswaldense contains two MipZ homologs, termed MipZ1 and MipZ2. MipZ2 localizes to the division site, but its absence does not cause any obvious phenotype. MipZ1, by contrast, forms a dynamic bipolar gradient, and its deletion or overproduction cause cell filamentation, suggesting an important role in cell division. The monomeric form of MipZ1 interacts with the chromosome partitioning protein ParB, whereas its ATP-dependent dimeric form shows non-specific DNA-binding activity. Notably, both the dimeric and, to a lesser extent, the monomeric form inhibit FtsZ polymerization in vitro. MipZ1 thus represents a canonical gradient-forming MipZ homolog that critically contributes to the spatiotemporal control of FtsZ ring formation. Collectively, our findings add to the view that the regulatory role of MipZ proteins in cell division is conserved among many alphaproteobacteria. However, their number and biochemical properties may have adapted to the specific needs of the host organism.

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Language(s): eng - English
 Dates: 2019
 Publication Status: Published in print
 Pages: 17
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 000487601400001
DOI: 10.1111/mmi.14369
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Title: MOLECULAR MICROBIOLOGY
Source Genre: Journal
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Publ. Info: 111 RIVER ST, HOBOKEN 07030-5774, NJ USA : WILEY
Pages: - Volume / Issue: 112 (5) Sequence Number: - Start / End Page: 1423 - 1439 Identifier: ISSN: 0950-382X