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<p>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 <i>Escherichia coli</i>, we show that the extreme N-terminal intrinsically disordered region (N-IDR) of FtsZ acts as a <i>cis</i> 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 <i>trans</i>-acting factors (such as the <i>E. coli</i> MinC protein).</p>

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

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2025年6月4日

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  • Huijia Yin,
  • Yang Liu,
  • Ying Zhao,
  • Pengyue Chen,
  • Zengyi Chang

摘要

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).