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Article

ZipA Uses a Two-Pronged FtsZ-Binding Mechanism Necessary for Cell Division.

mBio - 21 Dec 2021

Cameron Todd A, Vega Daniel E, Yu Chenfei, Xiao Han, Margolin William

Abstract excerpt

In most bacteria, cell division is centrally organized by the FtsZ protein, which assembles into dynamic filaments at the division site along the cell membrane that interact with other key cell division proteins. In gammaproteobacteria such as Escherichia coli, FtsZ filaments are anchored to the cell membrane by two essential proteins, FtsA and ZipA. Canonically, this interaction was believed to be mediated...

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Identifiers

PMID: 34903053
DOI: 10.1128/mbio.02529-21
PMCID: PMC8669495

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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

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ZipA Uses a Two-Pronged FtsZ-Binding Mechanism Necessary for Cell Division.PMID 34903053Read ↗

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 ↗

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

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

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

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 ↗

The bypass of ZipA by overexpression of FtsN requires a previously unknown conserved FtsN motif essential for FtsA-FtsN interaction supporting a model in which FtsA monomers recruit late cell division proteins to the Z 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 ↗

A role for the FtsQLB complex in cytokinetic ring activation revealed by an ftsL allele that accelerates division.Semantic proximity Read ↗

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