ArticleThe Journal of biological chemistry2015
Cytidine deaminase motifs within the DYW domain of two pentatricopeptide repeat-containing proteins are required for site-specific chloroplast RNA editing.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 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
52 citing papers in PubMed, 106 citations in OpenAlex.
- 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
- Synthetic Pentatricopeptide Repeat Proteins: Building a Toolkit for Precise RNA Control.International journal of molecular sciences · 2025Review
- First Identification of MORF Family in Ferns: Molecular Regulation of Organellar RNA Editing inBiology · 2025Article
- Deciphering the role of accessory proteins in Arabidopsis chloroplast editosomes via interaction with a synthetic PPR-PLS factor in E. coli.Nucleic acids research · 2025Article
- Pentatricopeptide repeat proteins in plants: Cellular functions, action mechanisms, and potential applications.Plant communications · 2025Review
- The Roles of MicroRNAs in the Regulation of Rice-Pathogen Interactions.Plants (Basel, Switzerland) · 2025Review
- Programmed RNA editing with an evolved bacterial adenosine deaminase.Nature chemical biology · 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
- Conservation of the moss RNA editing factor PPR78 despite the loss of its known cytidine-to-uridine editing sites is explained by a hidden extra target.The Plant cell · 2024Article
- Beyond a PPR-RNA recognition code: Many aspects matter for the multi-targeting properties of RNA editing factor PPR56.PLoS genetics · 2023Article
- A ribonuclease activity linked to DYW1 in vitro is inhibited by RIP/MORF proteins.Scientific reports · 2023Article
- Plant organellar RNA maturation.The Plant cell · 2023Review
- Structural insight into the activation of an Arabidopsis organellar C-to-U RNA editing enzyme by active site complementation.The Plant cell · 2023Article
- Genome-Wide Association Study Identified Novel SNPs Associated with Chlorophyll Content in Maize.Genes · 2023Article
- Emergence of Novel RNA-Editing Sites by Changes in the Binding Affinity of a Conserved PPR Protein.Molecular biology and evolution · 2022Article
- Exploring the RNA Editing Events and Their Potential Regulatory Roles in Tea Plant (International journal of molecular sciences · 2022Article
- Chloroplastic pentatricopeptide repeat proteins (PPR) in albino plantlets of Agave angustifolia Haw. reveal unexpected behavior.BMC plant biology · 2022Article
- Article
- An Insight Into Pentatricopeptide-Mediated Chloroplast NecrosisFrontiers in genetics · 2022Article
- DYW domain structures imply an unusual regulation principle in plant organellar RNA editing catalysis.Nature catalysis · 2021Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
In angiosperm organelles, cytidines are converted to uridines by a deamination reaction in the process termed RNA editing. The C targets of editing are recognized by members of the pentatricopeptide repeat (PPR) protein family. Although other members of the editosome have begun to be identified, the enzyme that catalyzes the C-U conversion is still unknown. The DYW motif at the C terminus of many PPR editing factors contains residues conserved with known cytidine deaminase active sites; however, some PPR editing factors lack a DYW motif. Furthermore, in many PPR-DYW editing factors, the truncation of the DYW motif does not affect editing efficiency, so the role of the DYW motif in RNA editing is unclear. Here, a chloroplast PPR-DYW editing factor, quintuple editing factor 1 (QED1), was shown to affect five different plastid editing sites, the greatest number of chloroplast C targets known to be affected by a single PPR protein. Loss of editing at the five sites resulted in stunted growth and accumulation of apparent photodamage. Adding a C-terminal protein tag to QED1 was found to severely inhibit editing function. QED1 and RARE1, another plastid PPR-DYW editing factor, were discovered to require their DYW motifs for efficient editing. To identify specific residues critical for editing, conserved deaminase residues in each PPR protein were mutagenized. The mutant PPR proteins, when expressed in qed1 or rare1 mutant protoplasts, could not complement the editing defect. Therefore, the DYW motif, and specifically, the deaminase residues, of QED1 and RARE1 are required for editing efficiency.
Indexed as
Identifiers
What Socratic 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 Socratic graph.