ArticleJournal of bacteriology2005
Cell division in Bacillus subtilis: FtsZ and FtsA association is Z-ring independent, and FtsA is required for efficient midcell Z-Ring assembly.
Article in Journal of bacteriology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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Who cites it
47 citing papers in PubMed.
- Defining the order of assembly of theJournal of bacteriology · 2026Article
- Human Milk Oligosaccharides Inhibit Group B Streptococcal Growth by Binding PcsB, an Essential Cell Wall Separation Protein.JACS Au · 2026Article
- Defining the order of assembly of thebioRxiv : the preprint server for biology · 2026Article
- Distinct modes of cell division drivemBio · 2025Article
- EzrA promotes Z-ring formation through interaction of its QNR motif with FtsA.Journal of bacteriology · 2025Article
- GpsB interacts with FtsZ in multiple species and may serve as an accessory Z-ring anchor.Molecular biology of the cell · 2025Article
- Staphylococcus aureus foldase PrsA contributes to the folding and secretion of protein A.BMC microbiology · 2024Article
- Comparing divisome organization between vegetative and sporulatingScience advances · 2024Article
- Models versus pathogens: how conserved is the FtsZ in bacteria?Bioscience reports · 2023Review
- Membrane mediated phase separation of the bacterial nucleoid occlusion protein Noc.Scientific reports · 2022Article
- Inhibition of Filamentous Thermosensitive Mutant-Z Protein inMolecules (Basel, Switzerland) · 2022Article
- Super-resolution confocal cryo-CLEM with cryo-FIB milling forCurrent research in structural biology · 2022Article
- The archaeal protein SepF is essential for cell division in Haloferax volcanii.Nature communications · 2021Article
- Single-molecule imaging reveals that Z-ring condensation is essential for cell division in Bacillus subtilis.Nature microbiology · 2021Article
- Structural Determinants and Their Role in Cyanobacterial Morphogenesis.Life (Basel, Switzerland) · 2020Review
- UbK is Involved in the Resistance of Bacillus Subtilis to Oxidative Stress.Current microbiology · 2020Article
- Enhancement of vitality and activity of a plant growth-promoting bacteria (PGPB) by atmospheric pressure non-thermal plasma.Scientific reports · 2019Article
- Single-Molecule Tracking of DNA Translocases in Bacillus subtilis Reveals Strikingly Different Dynamics of SftA, SpoIIIE, and FtsA.Applied and environmental microbiology · 2018Article
- The distinctive cell division interactome of Neisseria gonorrhoeae.BMC microbiology · 2017Article
- Free SepF interferes with recruitment of late cell division proteins.Scientific reports · 2017Article
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The earliest stage in cell division in bacteria is the assembly of a Z ring at the division site at midcell. Other division proteins are also recruited to this site to orchestrate the septation process. FtsA is a cytosolic division protein that interacts directly with FtsZ. Its function remains unknown. It is generally believed that FtsA localization to the division site occurs immediately after Z-ring formation or concomitantly with it and that FtsA is responsible for recruiting the later-assembling membrane-bound division proteins to the division site. Here, we report the development of an in vivo chemical cross-linking assay to examine the association between FtsZ and FtsA in Bacillus subtilis cells. We subsequently use this assay in a synchronous cell cycle to show that these two proteins can interact prior to Z-ring formation. We further show that in a B. subtilis strain containing an ftsA deletion, FtsZ localized at regular intervals along the filament but the majority of Z rings were abnormal. FtsA in this organism is therefore critical for the efficient formation of functional Z rings. This is the first report of abnormal Z-ring formation resulting from the loss of a single septation protein. These results suggest that in this organism, and perhaps others, FtsA ensures recruitment of the membrane-bound division proteins by ensuring correct formation of the Z ring.
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