ArticleJournal of bacteriology2014
The FtsZ-like protein FtsZm of Magnetospirillum gryphiswaldense likely interacts with its generic homolog and is required for biomineralization under nitrate deprivation.
Article in Journal of bacteriology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 36 citations in OpenAlex.
- Cross-linking proteomics analysis for reliable identification of MamXY-associated magnetosome formation.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2026Article
- Biosynthesis and function of magnetic organelles in magnetotactic bacteria.Nature reviews. Microbiology · 2026Review
- The transcriptomic landscape of Magnetospirillum gryphiswaldense during magnetosome biomineralization.BMC genomics · 2022Article
- The Complex Transcriptional Landscape of Magnetosome Gene Clusters in Magnetospirillum gryphiswaldense.mSystems · 2021Article
- Genome-Wide Identification of Essential and Auxiliary Gene Sets for Magnetosome Biosynthesis in Magnetospirillum gryphiswaldense.mSystems · 2020Article
- Magnetotactic Bacteria Accumulate a Large Pool of Iron Distinct from Their Magnetite Crystals.Applied and environmental microbiology · 2020Article
- A Compass To Boost Navigation: Cell Biology of Bacterial Magnetotaxis.Journal of bacteriology · 2020Review
- Magnetic genes: Studying the genetics of biomineralization in magnetotactic bacteria.PLoS genetics · 2020Review
- MamY is a membrane-bound protein that aligns magnetosomes and the motility axis of helical magnetotactic bacteria.Nature microbiology · 2019Article
- Agrobacterium tumefaciens divisome proteins regulate the transition from polar growth to cell division.Molecular microbiology · 2019Article
- Work Patterns of MamXY Proteins during Magnetosome Formation inApplied and environmental microbiology · 2019Article
- Prokaryotic cytoskeletons: protein filaments organizing small cells.Nature reviews. Microbiology · 2018Review
- Magnetosome biogenesis in magnetotactic bacteria.Nature reviews. Microbiology · 2016Review
- Dynamic Remodeling of the Magnetosome Membrane Is Triggered by the Initiation of Biomineralization.mBio · 2016Article
- From invagination to navigation: The story of magnetosome-associated proteins in magnetotactic bacteria.Protein science : a publication of the Protein Society · 2016Review
- The terminal oxidase cbb3 functions in redox control of magnetite biomineralization in Magnetospirillum gryphiswaldense.Journal of bacteriology · 2014Article
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8 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
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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