ArticleJournal of bacteriology2012
Identification of ZapD as a cell division factor that promotes the assembly of FtsZ in Escherichia coli.
Article in Journal of bacteriology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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Who cites it
71 citing papers in PubMed, 130 citations in OpenAlex.
- Article
- Article
- Crosslinking by ZapD drives the assembly of short FtsZ filaments into toroidal structures in solution.eLife · 2025Article
- Mycobacterial FtsZ and inhibitors: a promising target for the anti-tubercular drug development.Molecular diversity · 2024Review
- Computational andBiomedical reports · 2024Article
- The divisome is a self-enhancing machine in Escherichia coli and Caulobacter crescentus.Nature communications · 2024Article
- N-terminus GTPase domain of the cytoskeleton protein FtsZ plays a critical role in its adaptation to high hydrostatic pressure.Frontiers in microbiology · 2024Article
- Building the Bacterial Divisome at the Septum.Sub-cellular biochemistry · 2024Review
- FtsE, the Nucleotide Binding Domain of the ABC Transporter Homolog FtsEX, Regulates Septal PG Synthesis inMicrobiology spectrum · 2023Article
- Models versus pathogens: how conserved is the FtsZ in bacteria?Bioscience reports · 2023Review
- FtsZ phosphorylation pleiotropically affects Z-ladder formation, antibiotic production, and morphogenesis in Streptomyces coelicolor.Antonie van Leeuwenhoek · 2023Article
- Article
- Review
- Comparative Proteomics ofMicrobiology spectrum · 2022Article
- Localization, Assembly, and Activation of the Escherichia coli Cell Division Machinery.EcoSal Plus · 2021Review
- Simulations of Proposed Mechanisms of FtsZ-Driven Cell Constriction.Journal of bacteriology · 2021Article
- Article
- A Novel Z-Ring Associated Protein ZapA-Like Protein (PA5407) FromFrontiers in microbiology · 2021Article
- The Stress-Active Cell Division Protein ZapE Alters FtsZ Filament Architecture to Facilitate Division inFrontiers 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
11 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
The tubulin homolog FtsZ forms a polymeric membrane-associated ring structure (Z ring) at midcell that establishes the site of division and provides an essential framework for the localization of a multiprotein molecular machine that promotes division in Escherichia coli. A number of regulatory proteins interact with FtsZ and modulate FtsZ assembly/disassembly processes, ensuring the spatiotemporal integrity of cytokinesis. The Z-associated proteins (ZapA, ZapB, and ZapC) belong to a group of FtsZ-regulatory proteins that exhibit functionally redundant roles in stabilizing FtsZ-ring assembly by binding and bundling polymeric FtsZ at midcell. In this study, we report the identification of ZapD (YacF) as a member of the E. coli midcell division machinery. Genetics and cell biological evidence indicate that ZapD requires FtsZ but not other downstream division proteins for localizing to midcell, where it promotes FtsZ-ring assembly via molecular mechanisms that overlap with ZapA. Biochemical evidence indicates that ZapD directly interacts with FtsZ and promotes bundling of FtsZ protofilaments. Similarly to ZapA, ZapB, and ZapC, ZapD is dispensable for division and therefore belongs to the growing group of FtsZ-associated proteins in E. coli that aid in the overall fitness of the division process.
Indexed as
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.