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A FtsZ cis disassembly element acts in Z-ring assembly during bacterial cell division

Author

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  • Huijia Yin

    (Peking University
    Second Medical Center of Chinese PLA General Hospital)

  • Yang Liu

    (Peking University)

  • Ying Zhao

    (Peking University)

  • Pengyue Chen

    (Peking University)

  • Zengyi Chang

    (Peking University
    Peking University)

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).

Suggested Citation

  • Huijia Yin & Yang Liu & Ying Zhao & Pengyue Chen & Zengyi Chang, 2025. "A FtsZ cis disassembly element acts in Z-ring assembly during bacterial cell division," Nature Communications, Nature, vol. 16(1), pages 1-15, December.
    • Handle: RePEc:nat:natcom:v:16:y:2025:i:1:d:10.1038_s41467-025-60517-7
    DOI: 10.1038/s41467-025-60517-7
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