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<p>Bacterial RecA protein oligomerizes on single-stranded DNA (ssDNA) in the presence of ATP to form an active filament, RecA*, which is essential for homologous recombination and the activation of bacterial DNA damage response (SOS response). Despite extensive studies on the structure and function of RecA and RecA*, the exact function of the RecA flexible C-terminal tail remains poorly understood. Here, we report the crystal structure of the full-length RecA protein from <i>K. pneumoniae</i>, revealing that the C-terminal tail adopts a β-strand conformation. The negatively charged C-terminal tail is observed to interact with two positively charged conserved residues in the RecA core ATPase domain. We also demonstrate that the C-terminal tail of the <i>E. coli</i> and <i>K. pneumoniae</i> RecA inhibits the formation of RecA filament, DNA binding, and DNA strand exchange during homologous recombination, but promotes LexA self-cleavage as a co-protease and enhances the SOS response induced by mitomycin and ciprofloxacin. Our results provide mechanistic insights into the regulatory function of the RecA C-terminal tail in genome maintenance and DNA damage response.</p>

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Mechanistic insights into the structure and function of the RecA C-terminal tail

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2026年3月4日

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  • Lu Su,
  • Xiaofan Li,
  • Feifan Wang,
  • Mengzhen Wang,
  • Yimin Lu,
  • Yuyuan Zheng,
  • Anmin Gao,
  • Lu Chen,
  • Yajun Guo,
  • Mengchuan Xu,
  • Yu Feng,
  • Ning Dong,
  • Chun Zhou

摘要

Bacterial RecA protein oligomerizes on single-stranded DNA (ssDNA) in the presence of ATP to form an active filament, RecA*, which is essential for homologous recombination and the activation of bacterial DNA damage response (SOS response). Despite extensive studies on the structure and function of RecA and RecA*, the exact function of the RecA flexible C-terminal tail remains poorly understood. Here, we report the crystal structure of the full-length RecA protein from K. pneumoniae, revealing that the C-terminal tail adopts a β-strand conformation. The negatively charged C-terminal tail is observed to interact with two positively charged conserved residues in the RecA core ATPase domain. We also demonstrate that the C-terminal tail of the E. coli and K. pneumoniae RecA inhibits the formation of RecA filament, DNA binding, and DNA strand exchange during homologous recombination, but promotes LexA self-cleavage as a co-protease and enhances the SOS response induced by mitomycin and ciprofloxacin. Our results provide mechanistic insights into the regulatory function of the RecA C-terminal tail in genome maintenance and DNA damage response.