ArticleBiochemistry2012
Mg(2+)-linked self-assembly of FtsZ in the presence of GTP or a GTP analogue involves the concerted formation of a narrow size distribution of oligomeric species.
Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
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Who cites it
17 citing papers in PubMed, 23 citations in OpenAlex.
- The Diphosphoinositol Polyphosphate Phosphohydrolase 1 family binds IPInternational journal of biological macromolecules · 2026Article
- FtsZ Interactions and Biomolecular Condensates as Potential Targets for New Antibiotics.Antibiotics (Basel, Switzerland) · 2021Review
- Transient Membrane-Linked FtsZ Assemblies Precede Z-Ring Formation in Escherichia coli.Current biology : CB · 2020Article
- Dissipative adaptation in driven self-assembly leading to self-dividing fibrils.Nature nanotechnology · 2018Article
- Nucleotide and receptor density modulate binding of bacterial division FtsZ protein to ZipA containing lipid-coated microbeads.Scientific reports · 2017Article
- Self-Organization of FtsZ Polymers in Solution Reveals Spacer Role of the Disordered C-Terminal Tail.Biophysical journal · 2017Article
- Microenvironments created by liquid-liquid phase transition control the dynamic distribution of bacterial division FtsZ protein.Scientific reports · 2016Article
- Charged Molecules Modulate the Volume Exclusion Effects Exerted by Crowders on FtsZ Polymerization.PloS one · 2016Article
- The Cell Division Protein FtsZ from Streptococcus pneumoniae Exhibits a GTPase Activity Delay.The Journal of biological chemistry · 2015Article
- Evidence That Bacteriophage λ Kil Peptide Inhibits Bacterial Cell Division by Disrupting FtsZ Protofilaments and Sequestering Protein Subunits.The Journal of biological chemistry · 2015Article
- The Nucleoid Occlusion SlmA Protein Accelerates the Disassembly of the FtsZ Protein Polymers without Affecting Their GTPase Activity.PloS one · 2015Article
- Control by potassium of the size distribution of Escherichia coli FtsZ polymers is independent of GTPase activity.The Journal of biological chemistry · 2013Article
- MinC protein shortens FtsZ protofilaments by preferentially interacting with GDP-bound subunits.The Journal of biological chemistry · 2013Article
- Macromolecular interactions of the bacterial division FtsZ protein: from quantitative biochemistry and crowding to reconstructing minimal divisomes in the test tube.Biophysical reviews · 2013Review
- Light-scattering-based analysis of biomolecular interactions.Biophysical reviews · 2013Article
- Dynamic interaction of the Escherichia coli cell division ZipA and FtsZ proteins evidenced in nanodiscs.The Journal of biological chemistry · 2012Article
- An equilibrium model for the Mg(2+)-linked self-assembly of FtsZ in the presence of GTP or a GTP analogue.Biochemistry · 2012Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
The assembly of the bacterial cell division FtsZ protein in the presence of constantly replenished GTP was studied as a function of Mg(2+) concentration (at neutral pH and 0.5 M potassium) under steady-state conditions by sedimentation velocity, concentration-gradient light scattering, fluorescence correlation spectroscopy, and dynamic light scattering. Sedimentation velocity measurements confirmed previous results indicating cooperative appearance of a narrow size distribution of finite oligomers with increasing protein concentration. The concentration dependence of light scattering and diffusion coefficients independently verified the cooperative appearance of a narrow distribution of high molecular weight oligomers, and in addition provided a measurement of the average size of these species, which corresponds to 100 ± 20 FtsZ protomers at millimolar Mg(2+) concentration. Parallel experiments on solutions containing guanosine-5'-[(α,β)-methyleno]triphosphate, sodium salt (GMPCPP), a slowly hydrolyzable analogue of GTP, in place of GTP, likewise indicated the concerted formation of a narrow size distribution of fibrillar oligomers with a larger average mass (corresponding to 160 ± 20 FtsZ monomers). The closely similar behavior of FtsZ in the presence of both GTP and GMPCPP suggests that the observations reflect equilibrium rather than nonequilibrium steady-state properties of both solutions and exhibit parallel manifestations of a common association scheme.
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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.