ArticleThe Journal of biological chemistry2012
Dynamic interaction of the Escherichia coli cell division ZipA and FtsZ proteins evidenced in nanodiscs.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed.
- Fluorescence Correlation Spectroscopy to Examine Protein-Lipid Interactions in Membranes.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Protein-Protein Interactions as Promising Molecular Targets for Novel Antimicrobials Aimed at Gram-Negative Bacteria.International journal of molecular sciences · 2025Review
- Studying Macromolecular Interactions of Cellular Machines by the Combined Use of Analytical Ultracentrifugation, Light Scattering, and Fluorescence Spectroscopy Methods.Advances in experimental medicine and biology · 2024Article
- Biophysical Characterization of Membrane Proteins Embedded in Nanodiscs Using Fluorescence Correlation Spectroscopy.Membranes · 2022Review
- FtsZ Interactions and Biomolecular Condensates as Potential Targets for New Antibiotics.Antibiotics (Basel, Switzerland) · 2021Review
- FtsZ dynamics in bacterial division: What, how, and why?Current opinion in cell biology · 2021Review
- Functional Assembly ofBiomolecules · 2021Article
- Cell-free biogenesis of bacterial division proto-rings that can constrict liposomes.Communications biology · 2020Article
- Nano-encapsulated Escherichia coli Divisome Anchor ZipA, and in Complex with FtsZ.Scientific reports · 2019Article
- Surface Orientation and Binding Strength Modulate Shape of FtsZ on Lipid Surfaces.International journal of molecular sciences · 2019Article
- Escherichia coli ZipA Organizes FtsZ Polymers into Dynamic Ring-Like Protofilament Structures.mBio · 2018Article
- Nucleotide and receptor density modulate binding of bacterial division FtsZ protein to ZipA containing lipid-coated microbeads.Scientific reports · 2017Article
- Review
- Shape Selection of Surface-Bound Helical Filaments: Biopolymers on Curved Membranes.Biophysical journal · 2016Article
- Efficient Multiscale Models of Polymer Assembly.Biophysical journal · 2016Article
- Splitsville: structural and functional insights into the dynamic bacterial Z ring.Nature reviews. Microbiology · 2016Review
- Tuning the Photocycle Kinetics of Bacteriorhodopsin in Lipid Nanodiscs.Biophysical journal · 2015Article
- Article
- The Nucleoid Occlusion SlmA Protein Accelerates the Disassembly of the FtsZ Protein Polymers without Affecting Their GTPase Activity.PloS one · 2015Article
- Oligomerization of FtsZ converts the FtsZ tail motif (conserved carboxy-terminal peptide) into a multivalent ligand with high avidity for partners ZipA and SlmA.Molecular microbiology · 2015Article
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Authors and funding
9 authors.
Funding
Abstract
The full-length ZipA protein from Escherichia coli, one of the essential components of the division proto-ring that provides membrane tethering to the septation FtsZ protein, has been incorporated in single copy into nanodiscs formed by a membrane scaffold protein encircling an E. coli phospholipid mixture. This is an acellular system that reproduces the assembly of part of the cell division components. ZipA contained in nanodiscs (Nd-ZipA) retains the ability to interact with FtsZ oligomers and with FtsZ polymers. Interactions with FtsZ occur at similar strengths as those involved in the binding of the soluble form of ZipA, lacking the transmembrane region, suggesting that the transmembrane region of ZipA has little influence on the formation of the ZipA·FtsZ complex. Peptides containing partial sequences of the C terminus of FtsZ compete with FtsZ polymers for binding to Nd-ZipA. The affinity of Nd-ZipA for the FtsZ polymer formed with GTP or GMPCPP (a slowly hydrolyzable analog of GTP) is moderate (micromolar range) and of similar magnitude as for FtsZ-GDP oligomers. Polymerization does not stabilize the binding of FtsZ to ZipA. This supports the role of ZipA as a passive anchoring device for the proto-ring with little implication, if any, in the regulation of its assembly. Furthermore, it indicates that the tethering of FtsZ to the membrane shows sufficient plasticity to allow for its release from noncentral regions of the cytoplasmic membrane and its subsequent relocation to midcell when demanded by the assembly of a division ring.
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