ArticleJournal of bacteriology2011
Identification of Escherichia coli ZapC (YcbW) as a component of the division apparatus that binds and bundles FtsZ polymers.
Article in Journal of bacteriology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.
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Who cites it
67 citing papers in PubMed.
- Defining the order of assembly of theJournal of bacteriology · 2026Article
- The transcription factor Vca0578 (DsvR) mediated expression of ZapC is required to promote cell division during lytic transglycosylase insufficiency inbioRxiv : the preprint server for biology · 2026Article
- Defining the order of assembly of thebioRxiv : the preprint server for biology · 2026Article
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- Crosslinking by ZapD drives the assembly of short FtsZ filaments into toroidal structures in solution.eLife · 2025Article
- Comparative transcriptomics reveal stage-dependent parasitic adaptations in the myxozoan Sphaerospora molnari.BMC genomics · 2025Article
- The divisome is a self-enhancing machine in Escherichia coli and Caulobacter crescentus.Nature communications · 2024Article
- Unveiling the antibacterial mechanism of resveratrol againstFrontiers in cellular and infection microbiology · 2024Article
- Building the Bacterial Divisome at the Septum.Sub-cellular biochemistry · 2024Review
- Discovery and remodeling of Vibrio natriegens as a microbial platform for efficient formic acid biorefinery.Nature communications · 2023Article
- Pan-Genomics ofLife (Basel, Switzerland) · 2023Article
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- Early midcell localization of Escherichia coli PBP4 supports the function of peptidoglycan amidases.PLoS genetics · 2022Article
- Localization, Assembly, and Activation of the Escherichia coli Cell Division Machinery.EcoSal Plus · 2021Review
- Streptococcus suis MsmK: Novel Cell Division Protein Interacting with FtsZ and Maintaining Cell Shape.mSphere · 2021Article
- Simulations of Proposed Mechanisms of FtsZ-Driven Cell Constriction.Journal of bacteriology · 2021Article
- The Stress-Active Cell Division Protein ZapE Alters FtsZ Filament Architecture to Facilitate Division inFrontiers in microbiology · 2021Article
- A Novel Z-Ring Associated Protein ZapA-Like Protein (PA5407) FromFrontiers in microbiology · 2021Article
- Bacterial Vivisection: How Fluorescence-Based Imaging Techniques Shed a Light on the Inner Workings of Bacteria.Microbiology and molecular biology reviews : MMBR · 2020Review
7 more citing papers are in PubMed but not listed here.
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7 authors.
Funding
Abstract
Assembly of the cell division apparatus in bacteria starts with formation of the Z ring on the cytoplasmic face of the membrane. This process involves the accumulation of FtsZ polymers at midcell and their interaction with several FtsZ-binding proteins that collectively organize the polymers into a membrane-associated ring-like configuration. Three such proteins, FtsA, ZipA, and ZapA, have previously been identified in Escherichia coli. FtsA and ZipA are essential membrane-associated division proteins that help connect FtsZ polymers with the inner membrane. ZapA is a cytoplasmic protein that is not required for the fission process per se but contributes to its efficiency, likely by promoting lateral interactions between FtsZ protofilaments. We report the identification of YcbW (ZapC) as a fourth FtsZ-binding component of the Z ring in E. coli. Binding of ZapC promotes lateral interactions between FtsZ polymers and suppresses FtsZ GTPase activity. This and additional evidence indicate that, like ZapA, ZapC is a nonessential Z-ring component that contributes to the efficiency of the division process by stabilizing the polymeric form of FtsZ.
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