Publication Announcement: Unraveling the Structural Basis of the RNA Editing Mechanism by PPR-DYW Proteins
In a joint study with Kyushu University, we have successfully determined the three-dimensional structure of the PPR-DYW protein, responsible for C-to-U RNA editing in plants, for the first time in the world. This achievement lays a crucial foundation for more precise RNA editing technologies and drug discovery applications.
📋 Article Processing Timeline
- 📰 Published: May 15, 2026 at 00:30
- 🔍 Collected: May 14, 2026 at 16:02
- 🤖 AI Analyzed: May 15, 2026 at 04:26 (12h 23m after Collected)
We are pleased to announce that in a joint research project with Kyushu University, we have determined the three-dimensional structure of the PPR-DYW protein, which is responsible for C-to-U RNA editing in plants, for the first time in the world. The results were published in the British scientific journal 'Nature Communications' on April 27, 2026.
The PPR-DYW protein is composed of a 'PPR domain' that recognizes the target RNA sequence and a 'DYW domain' that rewrites the base. A long-standing challenge was to elucidate how these two domains coordinate to accurately edit only the target base. In this study, we successfully determined the crystal structures of the full-length protein, including both domains, in both RNA-unbound and bound states. This revealed the mechanism by which the protein undergoes a conformational change upon binding to the target RNA, accurately guiding the base to be edited to the catalytic center.
We are developing a programmable RNA editing technology called RECODE using PPR proteins. This achievement provides structural evidence for the high site-specificity of the PPR-DYW protein, establishing a foundation for the design of more precise RNA editing tools.
Moving forward, we will continue to advance research and development based on this achievement to further enhance the precision of RECODE technology and its application in drug discovery.
Publication Information
- Journal: Nature Communications
- Title: Structural basis of plant organelle C-to-U RNA editing by PPR-DYW proteins
- Authors: Takamasa Teramoto, Ryota Urushihara, Reiya Aoyama, Ayumi Okada, Mizuho Ichinose, Yusuke Yagi, Takahiro Nakamura, Bernard Gutmann, Yoshimitsu Kakuta
- Affiliations: Faculty of Agriculture, Kyushu University; EditForce, Inc.
- URL: https://doi.org/10.1038/s41467-026-72391-y
The PPR-DYW protein is composed of a 'PPR domain' that recognizes the target RNA sequence and a 'DYW domain' that rewrites the base. A long-standing challenge was to elucidate how these two domains coordinate to accurately edit only the target base. In this study, we successfully determined the crystal structures of the full-length protein, including both domains, in both RNA-unbound and bound states. This revealed the mechanism by which the protein undergoes a conformational change upon binding to the target RNA, accurately guiding the base to be edited to the catalytic center.
We are developing a programmable RNA editing technology called RECODE using PPR proteins. This achievement provides structural evidence for the high site-specificity of the PPR-DYW protein, establishing a foundation for the design of more precise RNA editing tools.
Moving forward, we will continue to advance research and development based on this achievement to further enhance the precision of RECODE technology and its application in drug discovery.
Publication Information
- Journal: Nature Communications
- Title: Structural basis of plant organelle C-to-U RNA editing by PPR-DYW proteins
- Authors: Takamasa Teramoto, Ryota Urushihara, Reiya Aoyama, Ayumi Okada, Mizuho Ichinose, Yusuke Yagi, Takahiro Nakamura, Bernard Gutmann, Yoshimitsu Kakuta
- Affiliations: Faculty of Agriculture, Kyushu University; EditForce, Inc.
- URL: https://doi.org/10.1038/s41467-026-72391-y