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<p>DNA-binding with one-finger (Dof) proteins are a family of plant-specific transcription factors distinguished by the highly conserved Dof DNA-binding domain. Various members play crucial roles in diverse plant biological processes. However, it remains unclear how the Dof domain recognizes a restricted set of promoters for gene regulation by binding to just four nucleotides, AAAG/CTTT. Here we present the crystal structure of the Dof domain of CYCLING DOF FACTOR 1 (CDF1), a well-characterized Dof protein acting as a transcriptional repressor by binding to the <i>CONSTANS</i> promoter to regulate photoperiodic flowering, in complex with DNA containing two <i>cis</i> elements. The data reveal that the Dof domain exhibits a unique zinc ribbon fold that includes a three-stranded antiparallel β-sheet and a carboxy-terminal loop, enabling DNA recognition accompanied by directional expansion of the major groove. These features facilitate binding to contiguous target <i>cis</i> elements in a proper arrangement to effectively regulate gene expression.</p>

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Structural insights into CDF1 accumulation on the CONSTANS promoter via a plant-specific DNA-binding domain

  • 期刊论文

  • 发表日期：

    2025年4月22日

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  • Hirotake Furihata,
  • Zhangliang Zhu,
  • Kaisei Nishida,
  • Yasuhito Sakuraba,
  • Akihiro Tsuji,
  • Hayato Yamashita,
  • Shohei Nosaki,
  • Ryo Tachibana,
  • Ayumi Yamagami,
  • Yoshiki Ikeda,
  • Masayuki Abe,
  • Tatsuya Sawasaki,
  • Takeshi Nakano,
  • Shuichi Yanagisawa,
  • Masaru Tanokura,
  • Takuya Miyakawa

摘要

DNA-binding with one-finger (Dof) proteins are a family of plant-specific transcription factors distinguished by the highly conserved Dof DNA-binding domain. Various members play crucial roles in diverse plant biological processes. However, it remains unclear how the Dof domain recognizes a restricted set of promoters for gene regulation by binding to just four nucleotides, AAAG/CTTT. Here we present the crystal structure of the Dof domain of CYCLING DOF FACTOR 1 (CDF1), a well-characterized Dof protein acting as a transcriptional repressor by binding to the CONSTANS promoter to regulate photoperiodic flowering, in complex with DNA containing two cis elements. The data reveal that the Dof domain exhibits a unique zinc ribbon fold that includes a three-stranded antiparallel β-sheet and a carboxy-terminal loop, enabling DNA recognition accompanied by directional expansion of the major groove. These features facilitate binding to contiguous target cis elements in a proper arrangement to effectively regulate gene expression.