ArticleMolecular microbiology2015
MinC/MinD copolymers are not required for Min function.
Article in Molecular microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
11 citing papers in PubMed.
- Membrane affinity difference between MinD monomer and dimer is not crucial for MinD gradient formation ineLife · 2026Article
- Building the Bacterial Divisome at the Septum.Sub-cellular biochemistry · 2024Review
- Insights into the assembly and regulation of the bacterial divisome.Nature reviews. Microbiology · 2024Review
- The E. coli MinCDE system in the regulation of protein patterns and gradients.Cellular and molecular life sciences : CMLS · 2019Review
- Cryo-EM structure of the MinCD copolymeric filament from Pseudomonas aeruginosa at 3.1 Å resolution.FEBS letters · 2019Article
- MinC N- and C-Domain Interactions Modulate FtsZ Assembly, Division Site Selection, and MinD-Dependent Oscillation inJournal of bacteriology · 2019Article
- The cell division protein MinD fromThe Journal of biological chemistry · 2018Article
- MinC and FtsZ mutant analysis provides insight into MinC/MinD-mediated Z ring disassembly.The Journal of biological chemistry · 2018Article
- Characterization of C-terminal structure of MinC and its implication in evolution of bacterial cell division.Scientific reports · 2017Article
- Structural Insights into Protein-Protein Interactions Involved in Bacterial Cell Wall Biogenesis.Antibiotics (Basel, Switzerland) · 2016Review
- Degradation of MinD oscillator complexes by Escherichia coli ClpXP.The Journal of biological chemistryArticle
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
In Escherichia coli, precise placement of the cytokinetic Z ring at midcell requires the concerted action of the three Min proteins. MinD activates MinC, an inhibitor of FtsZ, at least in part, by recruiting it to the membrane and targeting it to the Z ring, while MinE stimulates the MinD ATPase inducing an oscillation that directs MinC/MinD activity away from midcell. Recently, MinC and MinD were shown to form copolymers of alternating dimers of MinC and MinD, and it was suggested that these copolymers are the active form of MinC/MinD. Here, we use MinD mutants defective in binding MinC to generate heterodimers with wild-type MinD that are unable to form MinC/MinD copolymers. Similarly, MinC mutants defective in binding to MinD were used to generate heterodimers with wild-type MinC that are unable to form copolymers. Such heterodimers are active and in the case of MinC were shown to mediate spatial regulation of the Z ring demonstrating that MinC/MinD copolymer formation is not required. Our results are consistent with a model in which a membrane anchored MinC/MinD complex is targeted to the Z ring through the conserved carboxy tail of FtsZ leading to breakage of FtsZ filaments.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.