Download MendeleyStructural insights into CDF1 accumulation on the CONSTANS promoter via a plant-specific DNA-binding domain.
Furihata, H., Zhu, Z., Nishida, K., Sakuraba, Y., Tsuji, A., Yamashita, H., Nosaki, S., Tachibana, R., Yamagami, A., Ikeda, Y., Abe, M., Sawasaki, T., Nakano, T., Yanagisawa, S., Tanokura, M., Miyakawa, T.(2025) Nat Plants 11: 836-848
- PubMed: 40263610
- DOI: https://doi.org/10.1038/s41477-025-01946-6
- Primary Citation of Related Structures:
8XUF - PubMed Abstract:
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 ¦Â-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.
Organizational Affiliation:
Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Tokyo, Japan.
