ArticleMolecular microbiology2013
In vivo organization of the FtsZ-ring by ZapA and ZapB revealed by quantitative super-resolution microscopy.
Article in Molecular microbiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 90 papers.
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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.
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Who cites it
90 citing papers in PubMed, 151 citations in OpenAlex.
- Article
- Article
- Crosslinking by ZapD drives the assembly of short FtsZ filaments into toroidal structures in solution.eLife · 2025Article
- FtsZ-mediated spatial-temporal control over septal cell wall synthesis.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- A FtsZ cis disassembly element acts in Z-ring assembly during bacterial cell division.Nature communications · 2025Article
- Light-dependent modulation of protein localization and function in living bacteria cells.Nature communications · 2024Article
- The divisome is a self-enhancing machine in Escherichia coli and Caulobacter crescentus.Nature communications · 2024Article
- Distinct dynamics and proximity networks of hub proteins at the prey-invading cell pole in a predatory bacterium.Journal of bacteriology · 2024Article
- Protocol for single-molecule labeling and tracking of bacterial cell division proteins.STAR protocols · 2024Article
- Self-organization of mortal filaments and its role in bacterial division ring formation.Nature physics · 2024Article
- Building the Bacterial Divisome at the Septum.Sub-cellular biochemistry · 2024Review
- Application of nanotags and nanobodies for live cell single-molecule imaging of the Z-ring in Escherichia coli.Current genetics · 2023Article
- Bacterial division ring stabilizing ZapA versus destabilizing SlmA modulate FtsZ switching between biomolecular condensates and polymers.Open biology · 2023Article
- Three-dimensional coordination of cell-division site positioning in a filamentous cyanobacterium.PNAS nexus · 2023Article
- Cell wall synthesis and remodelling dynamics determine division site architecture and cell shape in Escherichia coli.Nature microbiology · 2022Article
- FtsN maintains active septal cell wall synthesis by forming a processive complex with the septum-specific peptidoglycan synthases in E. coli.Nature communications · 2022Article
- Single-molecule counting applied to the study of GPCR oligomerization.Biophysical journal · 2022Review
- Assembly dynamics of FtsZ and DamX during infection-related filamentation and division in uropathogenic E. coli.Nature communications · 2022Article
- Antibacterial activity of supernatants of Lactoccocus lactis, Lactobacillus rhamnosus, Pediococcus pentosaceus and curcumin against Aeromonas hydrophila. In vitro study.Veterinary research communications · 2022Article
- Exploration of Streptococcus core genome to reveal druggable targets and novel therapeutics against S. pneumoniae.PloS one · 2022Article
30 more citing papers are in PubMed but not listed here.
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
In most bacterial cells, cell division is dependent on the polymerization of the FtsZ protein to form a ring-like structure (Z-ring) at the midcell. Despite its essential role, the molecular architecture of the Z-ring remains elusive. In this work we examine the roles of two FtsZ-associated proteins, ZapA and ZapB, in the assembly dynamics and structure of the Z-ring in Escherichia coli cells. In cells deleted of zapA or zapB, we observed abnormal septa and highly dynamic FtsZ structures. While details of these FtsZ structures are difficult to discern under conventional fluorescence microscopy, single-molecule-based super-resolution imaging method Photoactivated Localization Microscopy (PALM) reveals that these FtsZ structures arise from disordered arrangements of FtsZ clusters. Quantitative analysis finds these clusters are larger and comprise more molecules than a single FtsZ protofilament, and likely represent a distinct polymeric species that is inherent to the assembly pathway of the Z-ring. Furthermore, we find these clusters are not due to the loss of ZapB-MatP interaction in ΔzapA and ΔzapB cells. Our results suggest that the main function of ZapA and ZapB in vivo may not be to promote the association of individual protofilaments but to align FtsZ clusters that consist of multiple FtsZ protofilaments.
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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.