ArticleThe Journal of biological chemistry2013
Identification of two pentatricopeptide repeat genes required for RNA editing and zinc binding by C-terminal cytidine deaminase-like domains.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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42 citing papers in PubMed, 83 citations in OpenAlex.
- Kingdom-wide evolutionary characterization of RNA editing factors in Archaeplastida.Molecular biology and evolution · 2026Article
- RNA-Binding Proteins in Dinoflagellates.International journal of molecular sciences · 2026Review
- 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
- The Roles of MicroRNAs in the Regulation of Rice-Pathogen Interactions.Plants (Basel, Switzerland) · 2025Review
- RNA Polymerase RPOTp is Involved in C-to-U RNA Editing at Multiple Sites in Arabidopsis Chloroplasts.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Transcriptome-wide Identification of Nine Tandem Repeat Protein Families in Roselle (Tropical life sciences research · 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
- RIP-Seq analysis of non-PPR chloroplast editing factors reveals broad RNA interactions and enrichment of less efficiently translated RNAs by OZ1 and ORRM1 complexes.The Plant journal : for cell and 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
- Structural insight into the activation of an Arabidopsis organellar C-to-U RNA editing enzyme by active site complementation.The Plant cell · 2023Article
- Plant organellar RNA maturation.The Plant cell · 2023Review
- A Comprehensive Evolutionary Study of Chloroplast RNA Editing in Gymnosperms: A Novel Type of G-to-A RNA Editing Is Common in Gymnosperms.International journal of molecular sciences · 2022Article
- Genetics of Fusarium head blight resistance in soft red winter wheat using a genome-wide association study.The plant genome · 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
- A synthetic RNA editing factor edits its target site in chloroplasts and bacteria.Communications biology · 2021Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Many transcripts expressed from plant organelle genomes are modified by C-to-U RNA editing. Nuclear encoded pentatricopeptide repeat (PPR) proteins are required as RNA binding specificity determinants in the RNA editing mechanism. Bioinformatic analysis has shown that most of the Arabidopsis PPR proteins necessary for RNA editing events include a C-terminal portion that shares structural characteristics with a superfamily of deaminases. The DYW deaminase domain includes a highly conserved zinc binding motif that shares characteristics with cytidine deaminases. The Arabidopsis PPR genes, ELI1 and DOT4, both have DYW deaminase domains and are required for single RNA editing events in chloroplasts. The ELI1 DYW deaminase domain was expressed as a recombinant protein in Escherichia coli and was shown to bind two zinc atoms per polypeptide. Thus, the DYW deaminase domain binds a zinc metal ion, as expected for a cytidine deaminase, and is potentially the catalytic component of an editing complex. Genetic complementation experiments demonstrate that large portions of the DYW deaminase domain of ELI1 may be eliminated, but the truncated genes retain the ability to restore editing site conversion in a mutant plant. These results suggest that the catalytic activity can be supplied in trans by uncharacterized protein(s) of the editosome.
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