Scholarlink

<p>Plants possess a unique C-to-U RNA editing mechanism mediated by PPR-DYW proteins, wherein the PPR domain recognizes specific RNA sequences while the DYW deaminase domain precisely edits the target C base—a process essential for functional protein expression in plant chloroplasts and mitochondria. The coordination of these two domains is considered crucial for precise RNA editing. In nature, this site-specific and precise base editing by PPR-DYW proteins distinguishes them from other base-editing deaminases. However, the absence of structures containing both PPR and DYW domains has limited our understanding of the precise RNA-editing mechanism of PPR-DYW proteins. Here, we present crystal structures of the consensus PPR-DYW (consPPR-DYW) protein, a representative of the PPR-DYW proteins, in both RNA-free and target RNA-bound states. Comparison between these states demonstrates domain movements upon target RNA binding, whereby the PPR domain accommodates the upstream sequence of the target C base in the proper conformation for editing while the DYW domain is optimally positioned for precise C-to-U conversion. These results, combined with comprehensive biochemical analyses, provide the foundation for a mechanistic model that explains the coordinated action of the PPR and DYW domains in achieving precise C-to-U editing.</p>

错误：搜索内容不能为空，请输入英文关键词
错误：关键词超出字数限制，请精简
高级检索

Structural basis of plant organelle C-to-U RNA editing by PPR-DYW proteins

  • 期刊论文

  • 出版模式：

    开放获取

  • 发表日期：

    2026年4月27日

查看全文
  • Takamasa Teramoto,
  • Ryota Urushihara,
  • Reiya Aoyama,
  • Ayumi Okada,
  • Mizuho Ichinose,
  • Yusuke Yagi,
  • Takahiro Nakamura,
  • Bernard Gutmann,
  • Yoshimitsu Kakuta

摘要

Plants possess a unique C-to-U RNA editing mechanism mediated by PPR-DYW proteins, wherein the PPR domain recognizes specific RNA sequences while the DYW deaminase domain precisely edits the target C base—a process essential for functional protein expression in plant chloroplasts and mitochondria. The coordination of these two domains is considered crucial for precise RNA editing. In nature, this site-specific and precise base editing by PPR-DYW proteins distinguishes them from other base-editing deaminases. However, the absence of structures containing both PPR and DYW domains has limited our understanding of the precise RNA-editing mechanism of PPR-DYW proteins. Here, we present crystal structures of the consensus PPR-DYW (consPPR-DYW) protein, a representative of the PPR-DYW proteins, in both RNA-free and target RNA-bound states. Comparison between these states demonstrates domain movements upon target RNA binding, whereby the PPR domain accommodates the upstream sequence of the target C base in the proper conformation for editing while the DYW domain is optimally positioned for precise C-to-U conversion. These results, combined with comprehensive biochemical analyses, provide the foundation for a mechanistic model that explains the coordinated action of the PPR and DYW domains in achieving precise C-to-U editing.