ArticleThe Journal of biological chemistry2017
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.
Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 47 citations in OpenAlex.
- 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
- Optimizing spatial organization of FtsZ rings for large-scale constriction in synthetic cells.Nature communications · 2026Article
- Article
- Crosslinking by ZapD drives the assembly of short FtsZ filaments into toroidal structures in solution.eLife · 2025Article
- Building the Bacterial Divisome at the Septum.Sub-cellular biochemistry · 2024Review
- N-terminus GTPase domain of the cytoskeleton protein FtsZ plays a critical role in its adaptation to high hydrostatic pressure.Frontiers in microbiology · 2024Article
- Models versus pathogens: how conserved is the FtsZ in bacteria?Bioscience reports · 2023Review
- Connecting sequence features within the disordered C-terminal linker ofProceedings of the National Academy of Sciences of the United States of America · 2022Article
- An enhancer sequence in the intrinsically disordered region of FtsZ promotes polymer-guided substrate processing by ClpXP protease.Protein science : a publication of the Protein Society · 2022Article
- Localization, Assembly, and Activation of the Escherichia coli Cell Division Machinery.EcoSal Plus · 2021Review
- The Stress-Active Cell Division Protein ZapE Alters FtsZ Filament Architecture to Facilitate Division inFrontiers in microbiology · 2021Article
- Molecular Characterization of theAntibiotics (Basel, Switzerland) · 2020Article
- Intrinsically Disordered Bacterial Polar Organizing Protein Z, PopZ, Interacts with Protein Binding Partners Through an N-terminal Molecular Recognition Feature.Journal of molecular biology · 2020Article
- A stochastic model for dynamics of FtsZ filaments and the formation of Z -ring.The European physical journal. E, Soft matter · 2020Article
- Essential dynamic interdependence of FtsZ and SepF for Z-ring and septum formation in Corynebacterium glutamicum.Nature communications · 2020Article
- Regulation of cytokinesis: FtsZ and its accessory proteins.Current genetics · 2020Review
- At the Heart of Bacterial Cytokinesis: The Z Ring.Trends in microbiology · 2019Review
- MinC N- and C-Domain Interactions Modulate FtsZ Assembly, Division Site Selection, and MinD-Dependent Oscillation inJournal of bacteriology · 2019Article
- Transcriptome analysis of the response of silkworm to drastic changes in ambient temperature.Applied microbiology and biotechnology · 2018Article
- Mapping the Contact Sites of theInternational journal of molecular sciences · 2018Article
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
Cell division in most bacteria is mediated by the tubulin-like FtsZ protein, which polymerizes in a GTP-dependent manner to form the cytokinetic Z ring. A diverse repertoire of FtsZ-binding proteins affects FtsZ localization and polymerization to ensure correct Z ring formation. Many of these proteins bind the C-terminal domain (CTD) of FtsZ, which serves as a hub for FtsZ regulation. FtsZ ring-associated proteins, ZapA-D (Zaps), are important FtsZ regulatory proteins that stabilize FtsZ assembly and enhance Z ring formation by increasing lateral assembly of FtsZ protofilaments, which then form the Z ring. There are no structures of a Zap protein bound to FtsZ; therefore, how these proteins affect FtsZ polymerization has been unclear. Recent data showed ZapD binds specifically to the FtsZ CTD. Thus, to obtain insight into the ZapD-CTD interaction and how it may mediate FtsZ protofilament assembly, we determined the
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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.