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Article

Genetic and biochemical characterization of the MinC-FtsZ interaction in Bacillus subtilis.

PloS one - 1 Jan 2013

Blasios Valdir, Bisson-Filho Alexandre W, Castellen Patricia, Nogueira Maria Luiza C, Bettini Jefferson, Portugal Rodrigo V, Zeri Ana Carolina M, Gueiros-Filho Frederico J

Abstract excerpt

Cell division in bacteria is regulated by proteins that interact with FtsZ and modulate its ability to polymerize into the Z ring structure. The best studied of these regulators is MinC, an inhibitor of FtsZ polymerization that plays a crucial role in the spatial control of Z ring formation. Recent work established that E. coli MinC interacts with two regions of FtsZ, the bottom face of the H10 helix and the...

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Identifiers

PMID: 23577149
DOI: 10.1371/journal.pone.0060690
PMCID: PMC3618327

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Genetic and biochemical characterization of the MinC-FtsZ interaction in Bacillus subtilis.PMID 23577149Read ↗

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

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

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

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

Effect of minCD on FtsZ ring position and polar septation in Bacillus subtilis.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 ↗

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

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

Bacillus subtilis SepF binds to the C-terminus of FtsZ.Semantic proximity Read ↗

SlmA antagonism of FtsZ assembly employs a two-pronged mechanism like MinCD.Semantic proximity Read ↗

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