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-spirals and -arcs determine the shape of the invaginating septa in some mutants of Escherichia coli.

Molecular microbiology - 1 Oct 1996

Addinall S G, Lutkenhaus J

Abstract excerpt

The essential cell division protein FtsZ forms a dynamic ring structure at the future division site. This Z-ring contracts during cell division while maintaining a position at the leading edge of the invaginating septum. Using immunofluorescence microscopy we have characterized two situations in which non-ring FtsZ structures are formed. In ftsZ26 (temperature sensitive, Ts) mutant cells, FtsZ-spirals are formed...

Read the complete abstract on PubMed

Topics

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

Share to Bacterial Proteins
Share to Cell Division
Share to Cytoskeletal Proteins

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Escherichia coli

Share to GTP-Binding Proteins

Share to Mutation

Share to Phenotype

Share to Temperature

Source

Identifiers

PMID: 8930908
DOI: 10.1046/j.1365-2958.1996.00100.x

Provenance

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.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

FtsZ-spirals and -arcs determine the shape of the invaginating septa in some mutants of Escherichia coli.PMID 8930908Read ↗

In vivo characterization of Escherichia coli ftsZ mutants: effects on Z-ring structure and function.Semantic proximity Read ↗

The bacterial cell division protein FtsZ assembles into cytoplasmic rings in fission yeast.Semantic proximity Read ↗

Assembly dynamics of FtsZ rings in Bacillus subtilis and Escherichia coli and effects of FtsZ-regulating proteins.Semantic proximity Read ↗

Temperature shift experiments with an ftsZ84(Ts) strain reveal rapid dynamics of FtsZ localization and indicate that the Z ring is required throughout septation and cannot reoccupy division sites once constriction has initiated.Semantic proximity Read ↗

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

Asymmetric cell division in B. subtilis involves a spiral-like intermediate of the cytokinetic protein FtsZ.Semantic proximity Read ↗

Influence of FtsZ GTPase activity and concentration on nanoscale Z-ring structure in vivo revealed by three-dimensional Superresolution imaging.Semantic proximity Read ↗

FtsZ ring formation in fts mutants.Semantic proximity Read ↗

Remodeling of the Z-Ring Nanostructure during the Streptococcus pneumoniae Cell Cycle Revealed by Photoactivated Localization MicroscopySemantic proximity Read ↗

Direct interaction of FtsZ and MreB is required for septum synthesis and cell division in Escherichia coli.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 ↗

RodZ (YfgA) is required for proper assembly of the MreB actin cytoskeleton and cell shape in E. coli.Semantic proximity Read ↗

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