ArticleThe Journal of biological chemistry2014
Self-assembly of MinE on the membrane underlies formation of the MinE ring to sustain function of the Escherichia coli Min system.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Growth-dependent concentration gradient of the oscillating Min system in Escherichia coli.The Journal of cell biology · 2025Article
- Probing Biomolecular Interactions by a Pattern-Forming Peptide-Conjugate Sensor.Bioconjugate chemistry · 2021Article
- C-terminal eYFP fusion impairsOpen biology · 2020Article
- MinE conformational switching confers robustness on self-organized Min protein patterns.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Mechanistic insights of the Min oscillator via cell-free reconstitution and imaging.Physical biology · 2018Review
- Dissecting the role of conformational change and membrane binding by the bacterial cell division regulator MinE in the stimulation of MinD ATPase activity.The Journal of biological chemistry · 2017Article
- MinE conformational dynamics regulate membrane binding, MinD interaction, and Min oscillation.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
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- Membrane-bound MinDE complex acts as a toggle switch that drives Min oscillation coupled to cytoplasmic depletion of MinD.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
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- The membrane: transertion as an organizing principle in membrane heterogeneity.Frontiers in microbiology · 2015Review
- Toward Spatially Regulated Division of Protocells: Insights into the E. coli Min System from in Vitro Studies.Life (Basel, Switzerland) · 2014Review
Corrections and comments
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The pole-to-pole oscillation of the Min proteins in Escherichia coli results in the inhibition of aberrant polar division, thus facilitating placement of the division septum at the midcell. MinE of the Min system forms a ring-like structure that plays a critical role in triggering the oscillation cycle. However, the mechanism underlying the formation of the MinE ring remains unclear. This study demonstrates that MinE self-assembles into fibrillar structures on the supported lipid bilayer. The MinD-interacting domain of MinE shows amyloidogenic properties, providing a possible mechanism for self-assembly of MinE. Supporting the idea, mutations in residues Ile-24 and Ile-25 of the MinD-interacting domain affect fibril formation, membrane binding ability of MinE and MinD, and subcellular localization of three Min proteins. Additional mutations in residues Ile-72 and Ile-74 suggest a role of the C-terminal domain of MinE in regulating the folding propensity of the MinD-interacting domain for different molecular interactions. The study suggests a self-assembly mechanism that may underlie the ring-like structure formed by MinE-GFP observed in vivo.
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