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

FtsZ-ZapA-ZapB interactome of Escherichia coli.

Journal of bacteriology - 1 Jan 2012

Galli Elisa, Gerdes Kenn

Abstract excerpt

Bacterial cell division relies on the formation and contraction of the Z ring, coordinated and regulated by a dynamic protein complex called the divisome. The cell division factor ZapA interacts directly with FtsZ and thereby increases FtsZ protofilament association and Z-ring stability. Here, we investigated ZapB interaction with ZapA and its effect on Z-ring formation and FtsZ protofilament bundling. The...

Read the complete abstract on PubMed

Topics

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

Share to Cell Cycle Proteins
Share to Cytokinesis
Share to Cytoskeletal Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Escherichia coli Proteins

Share to Gene Expression Regulation, Bacterial

Share to Green Fluorescent Proteins

Share to Hydrogen-Ion Concentration

Share to Plasmids

Source

Open in PubMed Open full text

Identifiers

PMID: 22056926
DOI: 10.1128/JB.05821-11
PMCID: PMC3256659

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

FtsZ-ZapA-ZapB interactome of Escherichia coli.PMID 22056926Read ↗

Structure and Mutational Analyses of Escherichia coli ZapD Reveal Charged Residues Involved in FtsZ Filament Bundling.Semantic proximity Read ↗

Structure of the Z Ring-associated Protein, ZapD, Bound to the C-terminal Domain of the Tubulin-like Protein, FtsZ, Suggests Mechanism of Z Ring Stabilization through FtsZ Cross-linking.Semantic proximity Read ↗

Bacterial division: the fellowship of the ring.Semantic proximity Read ↗

The In Vitro Non-Tetramerizing ZapAI83E Mutant Is Unable to Recruit ZapB to the Division Plane In Vivo in Escherichia coli.Semantic proximity Read ↗

FtsA Regulates Z-Ring Morphology and Cell Wall Metabolism in an FtsZ C-Terminal Linker-Dependent Manner in Caulobacter crescentus.Semantic proximity Read ↗

A mutation in Escherichia coli ftsZ bypasses the requirement for the essential division gene zipA and confers resistance to FtsZ assembly inhibitors by stabilizing protofilament bundling.Semantic proximity Read ↗

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

The ftsA* gain-of-function allele of Escherichia coli and its effects on the stability and dynamics of the Z ring.Semantic proximity Read ↗

GTPase activity regulates FtsZ ring positioning in Caulobacter crescentus.Semantic proximity Read ↗

Peptide Linkers within the Essential FtsZ Membrane Tethers ZipA and FtsA Are Nonessential for Cell Division.Semantic proximity Read ↗

Direct binding of FtsZ to ZipA, an essential component of the septal ring structure that mediates cell division in E. coli.Semantic proximity Read ↗

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