ArticleThe Journal of biological chemistry2012
MinD and MinE interact with anionic phospholipids and regulate division plane formation in Escherichia coli.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.
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54 citing papers in PubMed, 90 citations in OpenAlex.
- A lipid cue drives the subcellular localization of a self-inserting bacterial transmembrane protein.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Dark Side ofJournal of the American Chemical Society · 2026Article
- A lipid cue drives the subcellular localization of a self-inserting bacterial transmembrane protein.bioRxiv : the preprint server for biology · 2026Article
- Essential Role of LapD in the Absence of Cardiolipins.International journal of molecular sciences · 2026Article
- A surface-exposed cardiolipin synthase provides an unexpected paradigm for maintaining the Gram-negative outer membrane.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Marine-derived new peptaibols with antibacterial activities by targeting bacterial membrane phospholipids.Acta pharmaceutica Sinica. B · 2025Article
- Its own architect: Flipping cardiolipin synthase.Science advances · 2025Article
- Review
- Self-organized spatial targeting of contractile actomyosin rings for synthetic cell division.Nature communications · 2024Article
- Cell-free expression with a quartz crystal microbalance enables rapid, dynamic, and label-free characterization of membrane-interacting proteins.Communications biology · 2024Article
- Dynamic structure of E. coli cytoplasm: supramolecular complexes and cell aging impact spatial distribution and mobility of proteins.Communications biology · 2024Article
- Forceful patterning: theoretical principles of mechanochemical pattern formation.EMBO reports · 2023Review
- Article
- Multiparametric Sensing of Outer Membrane Vesicle-Derived Supported Lipid Bilayers Demonstrates the Specificity of Bacteriophage Interactions.ACS biomaterials science & engineering · 2023Article
- Turing-pattern model of scaffolding proteins that establish spatial asymmetry during the cell cycle ofiScience · 2023Article
- TTAPE-Me dye is not selective to cardiolipin and binds to common anionic phospholipids nonspecifically.Biophysical journal · 2021Article
- Cardiolipin-Containing Lipid Membranes Attract the Bacterial Cell Division Protein DivIVA.International journal of molecular sciences · 2021Article
- Increasing MinD's Membrane Affinity Yields Standing Wave Oscillations and Functional Gradients on Flat Membranes.ACS synthetic biology · 2021Article
- Cardiolipin aids in lipopolysaccharide transport to the gram-negative outer membrane.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Amphiphilic Aminoglycosides as Medicinal Agents.International journal of molecular sciences · 2020Review
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Min proteins (MinC, MinD, and MinE) form a pole-to-pole oscillator that controls the spatial assembly of the division machinery in Escherichia coli cells. Previous studies identified that interactions of MinD with phospholipids positioned the Min machinery at the membrane. We extend these studies by measuring the affinity, kinetics, and ATPase activity of E. coli MinD, MinE, and MinDE binding to supported lipid bilayers containing varying compositions of anionic phospholipids. Using quartz crystal microbalance measurements, we found that the binding affinity (K(d)) for the interaction of recombinant E. coli MinD and MinE with lipid bilayers increased with increasing concentration of the anionic phospholipids phosphatidylglycerol and cardiolipin. The K(d) for MinD (1.8 μM) in the presence of ATP was smaller than for MinE (12.1 μM) binding to membranes consisting of 95:5 phosphatidylcholine/cardiolipin. The simultaneous binding of MinD and MinE to membranes revealed that increasing the concentration of anionic phospholipid stimulates the initial rate of adsorption (k(on)). The ATPase activity of MinD decreased in the presence of anionic phospholipids. These results indicate that anionic lipids, which are concentrated at the poles, increase the retention of MinD and MinE and explain its dwell time at this region of bacterial cells. These studies provide insight into interactions between MinD and MinE and between these proteins and membranes that are relevant to understanding the process of bacterial cell division, in which the interaction of proteins and membranes is essential.
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