Identification and Characterization of ZapC, a Stabilizer of the FtsZ Ring in Escherichia coli
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Summary
The identification of an FtsZ stabilizer, ZapC (Z-associated protein C), in a protein localization screen conducted with E. coli suggests a key role for lateral bundling of the midcell Fts Z polymers in maintaining Ftsz ring stability during division.
- Type
- article
- Published
- 2011-01-07
- Cited by
- 126
- References
- 56
- OpenAlex
- https://openalex.org/W2129846745
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:11134796
Keywords
FtsZ, Cell division, Biology, Cytoskeleton, Cell biology
References
- Localization of FtsI (PBP3) to the Septal Ring Requires Its Membrane Anchor, the Z Ring, FtsA, FtsQ, and FtsL
- Towards Single-Copy Gene Expression Systems Making Gene Cloning Physiologically Relevant: Lambda InCh, a Simple Escherichia coli Plasmid-Chromosome Shuttle System
- Experiments With Gene Fusions
- Cross‐linking FtsZ polymers into coherent Z rings
- EzrA prevents aberrant cell division by modulating assembly of the cytoskeletal protein FtsZ
- Lateral FtsZ association and the assembly of the cytokinetic Z ring in bacteria
- Escherichia coli cell division protein FtsZ is a guanine nucleotide binding protein.
- ZipA is a MAP–Tau homolog and is essential for structural integrity of the cytokinetic FtsZ ring during bacterial cell division
- Escherichia coli cell-division gene ftsZ encodes a novel GTP-binding protein
- ZipA-Induced Bundling of FtsZ Polymers Mediated by an Interaction between C-Terminal Domains
- In Vivo Structure of the E. coli FtsZ-ring Revealed by Photoactivated Localization Microscopy (PALM)
- Protein interaction platforms: visualization of interacting proteins in yeast
- FtsZ polymer-bundling by the Escherichia coli ZapA orthologue, YgfE, involves a conformational change in bound GTP.
- FtsZ in Bacterial Cytokinesis: Cytoskeleton and Force Generator All in One
- Bacterial cell division: assembly, maintenance and disassembly of the Z ring
- The GTPase Activity of Escherichia coli FtsZ Determines the Magnitude of the FtsZ Polymer Bundling by ZapA in Vitro
- Polymerization of FtsZ, a Bacterial Homolog of Tubulin
- Reconstitution of Contractile FtsZ Rings in Liposomes
- FtsQ, FtsL and FtsI require FtsK, but not FtsN, for co‐localization with FtsZ during Escherichia coli cell division
- FtsZ exhibits rapid movement and oscillation waves in helix-like patterns in Escherichia coli.
Cited by
- ZapC promotes assembly and stability of FtsZ filaments by binding at a different site on FtsZ than ZipA.
- The C Terminus of FtsZ Regulates FtsZ Assembly Dynamics and Is Required for Bacillus subtilis Cell Division
- Cell division in Escherichia coli
- Structural and biochemical study of the proteins AmiC, NlpD and FtsW involved in the bacterial cell division
- Les systèmes Xer à une seule recombinase
- Identification of a novel cell division protein in Bacillus subtilis
- The structures, biological activity, and mechanistic studies of novel marine-derived antibacterial compounds
- Regulation of peptidoglycan synthesis during cell division in Escherichia coli
- Characterization of the cell division factor ZapB of Escherichia coli
- Identification and characterisation of cell division proteins in Staphylococcus aureus
- FtsA mutants impaired for self-interaction bypass ZipA suggesting a model in which FtsA's self-interaction competes with its ability to recruit downstream division proteins
- The ABC's of Cell Division: Regulation of Peptidoglycan Amidase Activity during Cytokinesis in Escherichia coli
- The Escherichia coli divisome: born to divide.
- Form and function of the bacterial cytokinetic ring.
- Cell wall architecture and the role of wall teichoic acid in Staphylococcus aureus
- Cell division in Corynebacterineae
- A Fail-Safe Mechanism in the Septal Ring Assembly Pathway Generated by the Sequential Recruitment of Cell Separation Amidases and Their Activators
- New(s) to the (Z-)ring.
- Bacillus subtilis SepF Binds to the C-Terminus of FtsZ
- The Escherichia coli cell division protein ZipA forms homodimers prior to association with FtsZ.
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