ArticleNucleic acids research2012
A pentatricopeptide repeat protein acts as a site-specificity factor at multiple RNA editing sites with unrelated cis-acting elements in plastids.
Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 50 citations in OpenAlex.
- Article
- Massive RNA Editing in Ascetosporean Mitochondria.Microbes and environments · 2025Article
- Plant mitochondrial RNA editing factors can perform targeted C-to-U editing of nuclear transcripts in human cells.Nucleic acids research · 2022Article
- PPR-DYW Protein EMP17 Is Required for Mitochondrial RNA Editing, Complex III Biogenesis, and Seed Development in Maize.Frontiers in plant science · 2021Article
- Yeast pentatricopeptide protein Dmr1 (Ccm1) binds a repetitive AU-rich motif in the small subunit mitochondrial ribosomal RNA.RNA (New York, N.Y.) · 2020Article
- Structural basis of mitochondrial translation.eLife · 2020Article
- Dynamic response of RNA editing to temperature in grape by RNA deep sequencing.Functional & integrative genomics · 2020Article
- Two organelle RNA recognition motif proteins affect distinct sets of RNA editing sites in thePlant direct · 2020Article
- Identification of soybean trans-factors associated with plastid RNA editing sites.Genetics and molecular biology · 2020Article
- The L motifs of two moss pentatricopeptide repeat proteins are involved in RNA editing but predominantly not in RNA recognition.PloS one · 2020Article
- RNA editing in the chloroplast of Asian Palmyra palm (Borassus flabellifer).Genetics and molecular biology · 2020Article
- GhYGL1d, a pentatricopeptide repeat protein, is required for chloroplast development in cotton.BMC plant biology · 2019Article
- Empty Pericarp21 encodes a novel PPR-DYW protein that is required for mitochondrial RNA editing at multiple sites, complexes I and V biogenesis, and seed development in maize.PLoS genetics · 2019Article
- The 27 kDa Trypanosoma brucei Pentatricopeptide Repeat Protein is a G-tract Specific RNA Binding Protein.Scientific reports · 2018Article
- A novel tetratricopeptide repeat protein, WHITE TO GREEN1, is required for early chloroplast development and affects RNA editing in chloroplasts.Journal of experimental botany · 2017Article
- In Silico Identification of Candidate Genes for Fertility Restoration in Cytoplasmic Male Sterile Perennial Ryegrass (Lolium perenne L.).Genome biology and evolution · 2017Article
- Distinct role of Arabidopsis mitochondrial P-type pentatricopeptide repeat protein-modulating editing protein, PPME, in nad1 RNA editing.RNA biology · 2016Article
- Predictable alteration of sequence recognition by RNA editing factors from Arabidopsis.The Plant cell · 2015Article
- Identification of two pentatricopeptide repeat genes required for RNA editing and zinc binding by C-terminal cytidine deaminase-like domains.The Journal of biological chemistry · 2013Article
- Mutagenesis of individual pentatricopeptide repeat motifs affects RNA binding activity and reveals functional partitioning of Arabidopsis PROTON gradient regulation3.The Plant cell · 2013Article
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In plant organelles, RNA editing alters specific cytidine residues to uridine in transcripts. All of the site-specificity factors of RNA editing identified so far are pentatricopeptide repeat (PPR) proteins. A defect in a specific PPR protein often impairs RNA editing at multiple sites, at which the cis-acting elements are not highly conserved. The molecular mechanism for sharing a single PPR protein over multiple sites is still unclear. We focused here on the PPR proteins OTP82 and CRR22, the putative target elements of which are, respectively, partially and barely conserved. Recombinant OTP82 specifically bound to the -15 to 0 regions of its target sites. Recombinant CRR22 specifically bound to the -20 to 0 regions of the ndhB-7 and ndhD-5 sites and to the -17 to 0 region of the rpoB-3 site. Taking this information together with the genetic data, we conclude that OTP82 and CRR22 act as site-specificity factors at multiple sites in plastids. In addition, the high-affinity binding of CRR22 to unrelated cis-acting elements suggests that only certain specific nucleotides in a cis-acting element are sufficient for high-affinity binding of a PPR protein. The cis-acting elements can therefore be rather divergent and still be recognized by a single PPR protein.
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