ArticlePloS one2012
Bacillus subtilis SepF binds to the C-terminus of FtsZ.
Article in PloS one, 2012. 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, 67 citations in OpenAlex.
- Molecular Mechanism of the SepF N‑Terminal Conformational Switch in Ring Assembly and Membrane Anchoring.JACS Au · 2026Article
- Distinct filament morphology and membrane tethering features of the dual FtsZ paralogs in Odinarchaeota.The EMBO journal · 2025Article
- Mycobacterial FtsZ and inhibitors: a promising target for the anti-tubercular drug development.Molecular diversity · 2024Review
- Comparing divisome organization between vegetative and sporulatingScience advances · 2024Article
- Anchors: A way for FtsZ filaments to stay membrane bound.Molecular microbiology · 2023Review
- Identification of anti-Acta pharmaceutica Sinica. B · 2023Article
- Models versus pathogens: how conserved is the FtsZ in bacteria?Bioscience reports · 2023Review
- FtsZ phosphorylation pleiotropically affects Z-ladder formation, antibiotic production, and morphogenesis in Streptomyces coelicolor.Antonie van Leeuwenhoek · 2023Article
- Review
- Methods for the Discovery and Identification of Small Molecules Targeting Oxidative Stress-Related Protein-Protein Interactions: An Update.Antioxidants (Basel, Switzerland) · 2022Review
- DNA damage checkpoint activation affects peptidoglycan synthesis and late divisome components in Bacillus subtilis.Molecular microbiology · 2021Article
- Review
- At the Heart of Bacterial Cytokinesis: The Z Ring.Trends in microbiology · 2019Review
- Free SepF interferes with recruitment of late cell division proteins.Scientific reports · 2017Article
- Structure of the Z Ring-associated Protein, ZapD, Bound to the C-terminal Domain of the Tubulin-like Protein, FtsZ, Suggests Mechanism of Z Ring Stabilization through FtsZ Cross-linking.The Journal of biological chemistry · 2017Article
- Review
- Splitsville: structural and functional insights into the dynamic bacterial Z ring.Nature reviews. Microbiology · 2016Review
- Structural and Functional Analyses Reveal Insights into the Molecular Properties of the Escherichia coli Z Ring Stabilizing Protein, ZapC.The Journal of biological chemistry · 2016Article
- Article
- HaloTag technology: a versatile platform for biomedical applications.Bioconjugate chemistry · 2015Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacterial cell division is mediated by a multi-protein machine known as the "divisome", which assembles at the site of cell division. Formation of the divisome starts with the polymerization of the tubulin-like protein FtsZ into a ring, the Z-ring. Z-ring formation is under tight control to ensure bacteria divide at the right time and place. Several proteins bind to the Z-ring to mediate its membrane association and persistence throughout the division process. A conserved stretch of amino acids at the C-terminus of FtsZ appears to be involved in many interactions with other proteins. Here, we describe a novel pull-down assay to look for binding partners of the FtsZ C-terminus, using a HaloTag affinity tag fused to the C-terminal 69 amino acids of B. subtilis FtsZ. Using lysates of Escherichia coli overexpressing several B. subtilis cell division proteins as prey we show that the FtsZ C-terminus specifically pulls down SepF, but not EzrA or MinC, and that the interaction depends on a conserved 16 amino acid stretch at the extreme C-terminus. In a reverse pull-down SepF binds to full-length FtsZ but not to a FtsZΔC16 truncate or FtsZ with a mutation of a conserved proline in the C-terminus. We show that the FtsZ C-terminus is required for the formation of tubules from FtsZ polymers by SepF rings. An alanine-scan of the conserved 16 amino acid stretch shows that many mutations affect SepF binding. Combined with the observation that SepF also interacts with the C-terminus of E. coli FtsZ, which is not an in vivo binding partner, we propose that the secondary and tertiary structure of the FtsZ C-terminus, rather than specific amino acids, are recognized by SepF.
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