ArticleThe Plant cell2023
Structural insight into the activation of an Arabidopsis organellar C-to-U RNA editing enzyme by active site complementation.
Article in The Plant cell, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Structural basis of plant organelle C-to-U RNA editing by PPR-DYW proteins.Nature communications · 2026Article
- Structures of pentatricopeptide repeat proteins.Acta crystallographica. Section F, Structural biology communications · 2026Review
- Genome-wide identification and dynamic transcriptome profiling of the DYW-type PPR family across greening of chlorotic leaves in pear (Frontiers in plant science · 2026Article
- RECODE: a programmable guide-free C-to-U RNA editing tool.Nucleic acids research · 2025Article
- De novo RNA base editing in plant organelles with engineered synthetic P-type PPR editing factors.Nucleic acids research · 2025Article
- Fine-tuning of the PPR protein directs the RNA editing activity toward C-to-U or U-to-C conversion.Scientific reports · 2025Article
- Pentatricopeptide repeat proteins in plants: Cellular functions, action mechanisms, and potential applications.Plant communications · 2025Review
- A Conserved Lysine in an Ion-Pair with a Catalytic Glutamate Is Critical for U-to-C RNA Editing but Restricts C-to-U RNA Editing.Biochemistry · 2025Article
- Seeing the unseen in characterizing RNA editome during rice endosperm development.Communications biology · 2024Article
- Multiple factors interact in editing of PPR-E+-targeted sites in maize mitochondria and plastids.Plant communications · 2024Article
- The dicot homolog of maize PPR103 carries a C-terminal DYW domain and may have a role in C-to-U editing of some chloroplast RNA transcripts.Plant molecular biology · 2024Article
- A ribonuclease activity linked to DYW1 in vitro is inhibited by RIP/MORF proteins.Scientific reports · 2023Article
- Focus on RNA biology.The Plant cell · 2023Article
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Authors and funding
7 authors.
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Abstract
RNA-binding pentatricopeptide repeat (PPR) proteins catalyze hundreds of cytidine to uridine RNA editing events in plant organelles; these editing events are essential for proper gene expression. More than half of the PPR-type RNA editing factors, however, lack the DYW cytidine deaminase domain. Genetic analyses have suggested that their cytidine deaminase activity arises by association with a family of DYW1-like proteins that contain an N-terminally truncated DYW domain, but their molecular mechanism has been unclear. Here, we report the crystal structure of the Arabidopsis thaliana DYW1 deaminase domain at 1.8 Å resolution. DYW1 has a cytidine deaminase fold lacking the PG box. The internal insertion within the deaminase fold shows an α-helical fold instead of the β-finger reported for the gating domain of the A. thaliana ORGANELLE TRANSCRIPT PROCESSING 86. The substrate-binding pocket is incompletely formed and appears to be complemented in the complex by the E2 domain and the PG box of the interacting PPR protein. In vivo RNA editing assays corroborate the activation model for DYW1 deaminase. Our study demonstrates the common activation mechanism of the DYW1-like proteins by molecular complementation of the DYW domain and reconstitution of the substrate-binding pocket.
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