ArticleJournal of bacteriology2005
MinC mutants deficient in MinD- and DicB-mediated cell division inhibition due to loss of interaction with MinD, DicB, or a septal component.
Article in Journal of bacteriology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed.
- Molecular and Structural Parallels between Gluten Pathogenic Peptides and Bacterial-Derived Proteins by Bioinformatics Analysis.International journal of molecular sciences · 2021Article
- Morphology engineering: a new strategy to construct microbial cell factories.World journal of microbiology & biotechnology · 2020Review
- Cryptic-Prophage-Encoded Small Protein DicB ProtectsJournal of bacteriology · 2019Article
- MinC N- and C-Domain Interactions Modulate FtsZ Assembly, Division Site Selection, and MinD-Dependent Oscillation inJournal of bacteriology · 2019Article
- Deciphering the Role of a SLOG Superfamily Protein YpsA in Gram-Positive Bacteria.Frontiers in microbiology · 2019Article
- Cross-Regulation between Bacteria and Phages at a Posttranscriptional Level.Microbiology spectrum · 2018Review
- 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
- 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
- Enhanced production of polyhydroxybutyrate by multiple dividing E. coli.Microbial cell factories · 2016Article
- Characterization of DicB by partially masking its potent inhibitory activity of cell division.Open biology · 2016Article
- MinC/MinD copolymers are not required for Min function.Molecular microbiology · 2015Article
- Insights into the cellular function of YhdE, a nucleotide pyrophosphatase from Escherichia coli.PloS one · 2015Article
- MinCD cell division proteins form alternating copolymeric cytomotive filaments.Nature communications · 2014Article
- Asymmetric constriction of dividing Escherichia coli cells induced by expression of a fusion between two min proteins.Journal of bacteriology · 2014Article
- Gene product 0.4 increases bacteriophage T7 competitiveness by inhibiting host cell division.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Crystal structure of the N-terminal domain of MinC dimerized via domain swapping.Journal of synchrotron radiation · 2013Article
- Genetic and biochemical characterization of the MinC-FtsZ interaction in Bacillus subtilis.PloS one · 2013Article
- Determination of the structure of the MinD-ATP complex reveals the orientation of MinD on the membrane and the relative location of the binding sites for MinE and MinC.Molecular microbiology · 2011Article
- Differences in MinC/MinD sensitivity between polar and internal Z rings in Escherichia coli.Journal of bacteriology · 2011Article
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Authors and funding
2 authors.
Funding
Abstract
The min locus encodes a negative regulatory system that limits formation of the cytokinetic Z ring to midcell by preventing its formation near the poles. Of the three Min proteins, MinC is the inhibitor and prevents Z-ring formation by interacting directly with FtsZ. MinD activates MinC by recruiting it to the membrane and conferring a higher affinity on the MinCD complex for a septal component. MinE regulates the cellular location of MinCD by inducing MinD, and thereby MinC, to oscillate between the poles of the cell, resulting in a time-averaged concentration of MinCD on the membrane that is lowest at midcell. MinC can also be activated by the prophage-encoded protein DicB, which targets MinC to the septum without recruiting it first to the membrane. Previous studies have shown that the C-terminal domain of MinC is responsible for the interaction with MinD, DicB, and the septal component. In the present study, we isolated mutations in the C-terminal domain of MinC that affected its interaction with MinD, DicB, and the septal component. Among the mutations isolated, R133A and S134A are specifically deficient in the interaction with MinD, E156A is primarily affected in the interaction with DicB, and R172A is primarily deficient in the interaction with the septum. These mutations differentiate the interactions of MinC with its partners and further support the model of MinCD- and MinC-DicB-mediated cell division inhibition.
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