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

Escherichia coli ZipA Organizes FtsZ Polymers into Dynamic Ring-Like Protofilament Structures.

mBio - 19 Jun 2018

Krupka Marcin, Sobrinos-Sanguino Marta, Jiménez Mercedes, Rivas Germán, Margolin William

Abstract excerpt

ZipA is an essential cell division protein in Escherichia coli Together with FtsA, ZipA tethers dynamic polymers of FtsZ to the cytoplasmic membrane, and these polymers are required to guide synthesis of the cell division septum. This dynamic behavior of FtsZ has been reconstituted on planar lipid surfaces in vitro, visible as GTP-dependent chiral vortices several hundred nanometers in diameter, when anchored by...

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 Cell Division
Share to Cell Membrane

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cytoskeletal Proteins

Share to Cytoskeleton

Share to Escherichia coli Proteins

Share to Guanosine Triphosphate

Share to Protein Multimerization

Source

Open in PubMed Open full text

Identifiers

PMID: 29921670
DOI: 10.1128/mBio.01008-18
PMCID: PMC6016244

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

Escherichia coli ZipA Organizes FtsZ Polymers into Dynamic Ring-Like Protofilament Structures.PMID 29921670Read ↗

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

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

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

Probing for Binding Regions of the FtsZ Protein Surface through Site-Directed Insertions: Discovery of Fully Functional FtsZ-Fluorescent Proteins.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 ↗

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

ZipA is a MAP-Tau homolog and is essential for structural integrity of the cytokinetic FtsZ ring during bacterial cell division.Semantic proximity Read ↗

A gain-of-function mutation in ftsA bypasses the requirement for the essential cell division gene zipA in Escherichia coli.Semantic proximity Read ↗

FtsZ-ZapA-ZapB interactome of Escherichia coli.Semantic proximity Read ↗

Dimer dynamics and filament organization of the bacterial cell division protein FtsA.Semantic proximity Read ↗

Unique and overlapping roles for ZipA and FtsA in septal ring assembly in Escherichia coli.Semantic proximity Read ↗

ZipA Uses a Two-Pronged FtsZ-Binding Mechanism Necessary for Cell Division.Semantic proximity Read ↗

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