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Article

MinC/MinD copolymers are not required for Min function.

Molecular microbiology - 1 Dec 2015

Park Kyung-Tae, Du Shishen, Lutkenhaus Joe

Abstract excerpt

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...

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Identifiers

PMID: 26268537
DOI: 10.1111/mmi.13164
PMCID: PMC4715711

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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MinC/MinD copolymers are not required for Min function.PMID 26268537Read ↗

MinCD cell division proteins form alternating copolymeric cytomotive filaments.Semantic proximity Read ↗

MinC and FtsZ mutant analysis provides insight into MinC/MinD-mediated Z ring disassembly.Semantic proximity Read ↗

The MinC component of the division site selection system in Escherichia coli interacts with FtsZ to prevent polymerization.Semantic proximity Read ↗

Assembly dynamics of the bacterial MinCDE system and spatial regulation of the Z ring.Semantic proximity Read ↗

Deletion of the min operon results in increased thermosensitivity of an ftsZ84 mutant and abnormal FtsZ ring assembly, placement, and disassembly.Semantic proximity Read ↗

Clostridial DivIVA and MinD interact in the absence of MinJ.Semantic proximity Read ↗

Characterization of ftsZ mutations that render Bacillus subtilis resistant to MinC.Semantic proximity Read ↗

MinC mutants deficient in MinD- and DicB-mediated cell division inhibition due to loss of interaction with MinD, DicB, or a septal component.Semantic proximity Read ↗

Bacillus subtilis MinC destabilizes FtsZ-rings at new cell poles and contributes to the timing of cell division.Semantic proximity Read ↗

The Division Defect of a Bacillus subtilis minD noc Double Mutant Can Be Suppressed by Spx-Dependent and Spx-Independent Mechanisms.Semantic proximity Read ↗

Min oscillation in bacteria.Semantic proximity Read ↗

The switch I and II regions of MinD are required for binding and activating MinC.Semantic proximity Read ↗

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