ArticleNature communications2025
A FtsZ cis disassembly element acts in Z-ring assembly during bacterial cell division.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed.
- Berberine Hydrochloride Attenuates Growth, Biofilm Formation, and Virulence Associated Phenotypes of Actinobacillus pleuropneumoniae Strain APP-2023.Current microbiology · 2026Article
- Article
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5 authors.
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Abstract
Bacterial cell division hinges on the Z-ring, an architecture built from the dynamical assembly and disassembly of FtsZ proteins. This delicate balance ensures not only apparent stability, but also continuous remodeling, both of which are required for Z-ring functioning. However, the molecular nature of such subcellular structures remains elusive. Here, by identifying all amino acid residues participating in FtsZ self-assembly in Escherichia coli, we show that the extreme N-terminal intrinsically disordered region (N-IDR) of FtsZ acts as a cis disassembly element that contacts and disrupts the longitudinal interface, tipping the balance more toward polymer disassembly. This previously unappreciated structural characteristic is indispensable for promoting Z-ring architecture condensation at midcell (rather than elsewhere) upon modulation by certain trans-acting factors (such as the E. coli MinC protein).
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