Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

MinCD cell division proteins form alternating copolymeric cytomotive filaments.

Nature communications - 15 Dec 2014

Ghosal Debnath, Trambaiolo Daniel, Amos Linda A, Löwe Jan

Abstract excerpt

During bacterial cell division, filaments of the tubulin-like protein FtsZ assemble at midcell to form the cytokinetic Z-ring. Its positioning is regulated by the oscillation of MinCDE proteins. MinC is activated by MinD through an unknown mechanism and prevents Z-ring assembly anywhere but midcell. Here, using X-ray crystallography, electron microscopy and in vivo analyses, we show that MinD activates MinC by...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Adenosine Triphosphatases
Share to Crystallography, X-Ray
Share to Cytoskeletal Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cytoskeleton

Share to Genes, Reporter

Share to Liposomes

Share to Microscopy, Electron

Share to Polymerization

Source

Open in PubMed Open full text

Identifiers

PMID: 25500731
DOI: 10.1038/ncomms6341
PMCID: PMC4338524

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

MinCD cell division proteins form alternating copolymeric cytomotive filaments.PMID 25500731Read ↗

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

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

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 ↗

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

A plant MinD homologue rescues Escherichia coli HL1 mutant (DeltaMinDE) in the absence of MinE.Semantic proximity Read ↗

Min oscillation in bacteria.Semantic proximity Read ↗

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

A multistranded polymer model explains MinDE dynamics in E. coli cell division.Semantic proximity Read ↗

MinE conformational dynamics regulate membrane binding, MinD interaction, and Min oscillation.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.