ArticleNature communications2020
Essential dynamic interdependence of FtsZ and SepF for Z-ring and septum formation in Corynebacterium glutamicum.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed.
- Deep learning extracts MoA-specific signatures from high-throughput images of chemically and genetically perturbedScience advances · 2026Article
- Defining the order of assembly of theJournal of bacteriology · 2026Article
- Molecular Mechanism of the SepF N‑Terminal Conformational Switch in Ring Assembly and Membrane Anchoring.JACS Au · 2026Article
- Functional dissection ofmBio · 2026Article
- Functional flexibility in bacterial hub proteins is driven by proteome expansion.Scientific reports · 2026Article
- Article
- Defining the order of assembly of thebioRxiv : the preprint server for biology · 2026Article
- Distinct filament morphology and membrane tethering features of the dual FtsZ paralogs in Odinarchaeota.The EMBO journal · 2025Article
- A strategy to re-sensitise drug-resistant Gram-positive bacteria to oxazolidinone-class antibiotics.EBioMedicine · 2025Article
- Cryo-EM structure and polar assembly of the PS2 S-layer ofProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Cell division protein CdpA organises and anchors the midcell ring in haloarchaea.Nature communications · 2025Article
- Membrane Association of Intrinsically Disordered Proteins.Annual review of biophysics · 2025Review
- Article
- Article
- GpsB interacts with FtsZ in multiple species and may serve as an accessory Z-ring anchor.Molecular biology of the cell · 2025Article
- Tip extension and simultaneous multiple fission in a filamentous bacterium.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Proteins containing photosynthetic reaction centre domains modulate FtsZ-based archaeal cell division.Nature microbiology · 2024Article
- Molecular basis for curvature formation in SepF polymerization.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Creating Polyploid Escherichia Coli and Its Application in Efficient L-Threonine Production.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Article
- Eukaryotic-like gephyrin and cognate membrane receptor coordinate corynebacterial cell division and polar elongation.Nature microbiology · 2023Article
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Authors and funding
14 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The mechanisms of Z-ring assembly and regulation in bacteria are poorly understood, particularly in non-model organisms. Actinobacteria, a large bacterial phylum that includes the pathogen Mycobacterium tuberculosis, lack the canonical FtsZ-membrane anchors and Z-ring regulators described for E. coli. Here we investigate the physiological function of Corynebacterium glutamicum SepF, the only cell division-associated protein from Actinobacteria known to interact with the conserved C-terminal tail of FtsZ. We show an essential interdependence of FtsZ and SepF for formation of a functional Z-ring in C. glutamicum. The crystal structure of the SepF-FtsZ complex reveals a hydrophobic FtsZ-binding pocket, which defines the SepF homodimer as the functional unit, and suggests a reversible oligomerization interface. FtsZ filaments and lipid membranes have opposing effects on SepF polymerization, indicating that SepF has multiple roles at the cell division site, involving FtsZ bundling, Z-ring tethering and membrane reshaping activities that are needed for proper Z-ring assembly and function.
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