Publication Announcement: Structural Basis of the RNA Editing Mechanism of PPR-DYW Proteins Revealed
EditForce, Inc. is pleased to announce that, through a collaborative study with Kyushu University, it has elucidated for the first time the three-dimensional structure of a PPR-DYW protein responsible for C-to-U RNA editing in plants. The results were published in Nature Communications on April 27, 2026.
PPR-DYW proteins consist of a PPR domain that recognizes the target RNA sequence and a DYW domain that catalyzes base conversion. How these two domains coordinate to precisely edit only the target base has been a long-standing question in the field. In this study, crystal structures of the full-length protein containing both domains were determined in both RNA-free and RNA-bound states, revealing the mechanism by which target RNA binding induces a conformational change in the protein and precisely guides the base to be edited into the catalytic center.
EditForce is developing programmable RNA editing technology (RECODE) based on PPR proteins. These findings provide structural support for the high site-specificity of PPR-DYW proteins and establish a foundation for designing more precise RNA editing tools.
Building on these results, EditForce will continue to improve the precision of its RECODE technology and advance research and development toward drug discovery applications.
Publication Details:
- 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