ArticleMolecular microbiology2012
FtsA mutants impaired for self-interaction bypass ZipA suggesting a model in which FtsA's self-interaction competes with its ability to recruit downstream division proteins.
Article in Molecular microbiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.
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Who cites it
75 citing papers in PubMed.
- Control of cell division by anbioRxiv : the preprint server for biology · 2026Article
- Determining the rate-limiting processes for cell division in Escherichia coli.Nature communications · 2024Article
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- Article
- Role of the antiparallel double-stranded filament form of FtsA in activating thebioRxiv : the preprint server for biology · 2024Article
- Insights into the assembly and regulation of the bacterial divisome.Nature reviews. Microbiology · 2024Review
- Anchors: A way for FtsZ filaments to stay membrane bound.Molecular microbiology · 2023Review
- Construction and Characterization of Functional FtsA Sandwich Fusions for Studies of FtsA Localization and Dynamics during Escherichia coli Cell Division.Journal of bacteriology · 2023Article
- Bacterial divisome protein FtsA forms curved antiparallel double filaments when binding to FtsN.Nature microbiology · 2022Article
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- Min waves without MinC can pattern FtsA-anchored FtsZ filaments on model membranes.Communications biology · 2022Article
- In vitro reconstitution of Escherichia coli divisome activation.Nature communications · 2022Article
- An Updated Model of the Divisome: Regulation of the Septal Peptidoglycan Synthesis Machinery by the Divisome.International journal of molecular sciences · 2022Review
- Localization, Assembly, and Activation of the Escherichia coli Cell Division Machinery.EcoSal Plus · 2021Review
- TheInternational journal of molecular sciences · 2021Article
- FtsA acts through FtsW to promote cell wall synthesis during cell division inProceedings of the National Academy of Sciences of the United States of America · 2021Article
- FtsZ dynamics in bacterial division: What, how, and why?Current opinion in cell biology · 2021Review
- Bacterial cell proliferation: from molecules to cells.FEMS microbiology reviews · 2021Review
- Assembly properties of bacterial tubulin homolog FtsZ regulated by the positive regulator protein ZipA and ZapA from Pseudomonas aeruginosa.Scientific reports · 2020Article
- Cell-free biogenesis of bacterial division proto-rings that can constrict liposomes.Communications biology · 2020Article
15 more citing papers are in PubMed but not listed here.
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4 authors.
Funding
Abstract
Z-ring assembly requires polymers of the tubulin homologue FtsZ to be tethered to the membrane. Although either ZipA or FtsA is sufficient to do this, both of these are required for recruitment of downstream proteins to form a functional cytokinetic ring. Gain of function mutations in ftsA, such as ftsA* (ftsA-R286W), bypass the requirement for ZipA suggesting that this atypical, well-conserved, actin homologue has a more critical role in Z-ring function. FtsA forms multimers both in vitro and in vivo, but little is known about the role of FtsA polymerization. In this study we identify FtsA mutants impaired for self-interaction. Such mutants are able to support Z-ring assembly and are also able to bypass the requirement for ZipA. These mutants, including FtsA*, have reduced ability to self-interact but interact normally with FtsZ and are less toxic if overexpressed. These results do not support a model in which FtsA monomers antagonize FtsZ polymers. Instead, we propose a new model in which FtsA self-interaction competes with its ability to recruit downstream proteins. In this model FtsA self-interaction at the Z ring is antagonized by ZipA, allowing unpolymerized FtsA to recruit downstream proteins such as FtsN.
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