ArticleScientific reports2025
Fine-tuning of the PPR protein directs the RNA editing activity toward C-to-U or U-to-C conversion.
Article in Scientific reports, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
3 citing papers in PubMed.
- A Generalized AI View of Tricopeptide Repeats: What's in a Name.International journal of molecular sciences · 2025Review
- GRASP: a modular toolkit for building synthetic pentatricopeptide repeat RNA-binding proteins.Nucleic acids research · 2025Article
- High Conservation of Translation-Enabling RNA Editing Sites in Hyper-editing Ferns Implies They Are Not Selectively Neutral.Molecular biology and evolution · 2025Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A subfamily of pentatricopeptide repeat (PPR) proteins, known as PPR-DYW:PG, catalyzes the cytidine to uridine (C-to-U) RNA editing in plant organelles. A related PPR subfamily, PPR-DYW:KP, catalyzes the uridine to cytidine (U-to-C) reaction, via a crosslinking mechanism involving a lysine residue. We demonstrate that Lys88 in the DYW:KP domain is essential for the U-to-C editing activity of PPR-DYW:KP proteins. Substituting Lys88 with other amino acids in designer proteins switches the protein activity to C-to-U and prevents crosslinking with the edited RNA. However, this mutation leads to C-to-U off-target editing downstream the targeted site. Finally, other modifications can modulate the catalytic activity and alter the type of reaction catalyzed by the DYW domain. Altogether, our results suggest that subtle modifications in the DYW domain can influence the position of the edited nucleotide and the type of RNA editing reaction.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.