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Article

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

Proceedings of the National Academy of Sciences of the United States of America - 21 Dec 1999

Hu Z, Mukherjee A, Pichoff S, Lutkenhaus J

Abstract excerpt

Positioning of the Z ring at the midcell site in Escherichia coli is assured by the min system, which masks polar sites through topological regulation of MinC, an inhibitor of division. To study how MinC inhibits division, we have generated a MalE-MinC fusion that retains full biological activity. We find that MalE-MinC interacts with FtsZ and prevents polymerization without inhibiting FtsZ's GTPase activity....

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Identifiers

PMID: 10611296
DOI: 10.1073/pnas.96.26.14819
PMCID: PMC24731

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Source receipt: pubmed, retrieved 7 Sept 2026.

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Research trail→

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The MinC component of the division site selection system in Escherichia coli interacts with FtsZ to prevent polymerization.PMID 10611296Read ↗

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

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

Genetic and biochemical characterization of the MinC-FtsZ interaction in Bacillus subtilis.Semantic proximity Read ↗

Escherichia coli division inhibitor MinCD blocks septation by preventing Z-ring formation.Semantic proximity Read ↗

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

MinJ (YvjD) is a topological determinant of cell division in Bacillus subtilis.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 ↗

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 ↗

MinC/MinD copolymers are not required for Min function.Semantic proximity Read ↗

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

FtsZ ring clusters in min and partition mutants: role of both the Min system and the nucleoid in regulating FtsZ ring localization.Semantic proximity Read ↗

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