ArticleProceedings of the National Academy of Sciences of the United States of America2007
Conserved domain structure of pentatricopeptide repeat proteins involved in chloroplast RNA editing.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 123 papers.
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123 citing papers in PubMed, 272 citations in OpenAlex.
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- The Roles of MicroRNAs in the Regulation of Rice-Pathogen Interactions.Plants (Basel, Switzerland) · 2025Review
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- Proteomic profiling ofPhysiology and molecular biology of plants : an international journal of functional plant biology · 2024Article
- A Bibliometric Study for Plant RNA Editing Research: Trends and Future Challenges.Molecular biotechnology · 2023Review
- Structural insight into the activation of an Arabidopsis organellar C-to-U RNA editing enzyme by active site complementation.The Plant cell · 2023Article
- Characterization of theGenes · 2023Article
- De Novo Transcriptome Assembly and Comparative Analysis of Differentially Expressed Genes Involved in Cold Acclimation and Freezing Tolerance of the Arctic MossPlants (Basel, Switzerland) · 2023Article
- Grafting enhances drought tolerance by regulating and mobilizing proteome, transcriptome and molecular physiology in okra genotypes.Frontiers in plant science · 2023Article
- 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
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- An overview of RNA splicing and functioning of splicing factors in land plant chloroplasts.RNA biology · 2022Article
- An Insight Into Pentatricopeptide-Mediated Chloroplast NecrosisFrontiers in genetics · 2022Article
- Genome-wide analysis uncovers tomato leaf lncRNAs transcriptionally active upon Pseudomonas syringae pv. tomato challenge.Scientific reports · 2021Article
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- DYW domain structures imply an unusual regulation principle in plant organellar RNA editing catalysis.Nature catalysis · 2021Article
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- Article
63 more citing papers are in PubMed but not listed here.
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5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The pentatricopeptide repeat (PPR) proteins form one of the largest families in higher plants and are believed to be involved in the posttranscriptional processes of gene expression in plant organelles. It has been shown by using a genetic approach focusing on NAD(P)H dehydrogenase (NDH) activity that a PPR protein CRR4 is essential for a specific RNA editing event in chloroplasts. Here, we discovered Arabidopsis crr21 mutants that are specifically impaired in the RNA editing of the site 2 of ndhD (ndhD-2), which encodes a subunit of the NDH complex. The CRR21 gene encodes a member of the PPR protein family. The RNA editing of ndhD-2 converts the Ser-128 of NdhD to leucine. In crr21, the activity of the NDH complex is specifically impaired, suggesting that the Ser128Leu change has important consequences for the function of the NDH complex. Both CRR21 and CRR4 belong to the E+ subgroup in the PLS subfamily that is characterized by the presence of a conserved C-terminal region (the E/E+ domain). This E/E+ domain is highly conserved and exchangeable between CRR21 and CRR4, although it is not essential for the RNA binding. Our results suggest that the E/E+ domain has a common function in RNA editing rather than of recognizing specific RNA sequences.
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