ArticlePloS one2013
Elucidation of the RNA recognition code for pentatricopeptide repeat proteins involved in organelle RNA editing in plants.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 157 papers.
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Who cites it
157 citing papers in PubMed, 290 citations in OpenAlex.
- Pentatricopeptide repeat proteins in crops: Advances in functional mechanisms and breeding applications.Journal of integrative plant biology · 2026Review
- Expanding the palette of cis-elements to tune the expression of chloroplast transgenes in tobacco.The Plant journal : for cell and molecular biology · 2026Article
- PCIS1 is an essential factor in mitochondrial RNA splicing and complex I biogenesis, with distinct effects in null and downregulated mutants.Plant cell reports · 2026Article
- Structural basis of plant organelle C-to-U RNA editing by PPR-DYW proteins.Nature communications · 2026Article
- Structures of pentatricopeptide repeat proteins.Acta crystallographica. Section F, Structural biology communications · 2026Review
- Natural Variation of a PPR Coding Gene SST1 Confers Salt Tolerance During Soybean Domestication.Plant biotechnology journal · 2026Article
- Integrated analysis of organelle RNA editing and DYW- type PPR genes identifies a candidate regulator of plastidFrontiers in plant science · 2026Article
- Synthetic Pentatricopeptide Repeat Proteins: Building a Toolkit for Precise RNA Control.International journal of molecular sciences · 2025Review
- A Generalized AI View of Tricopeptide Repeats: What's in a Name.International journal of molecular sciences · 2025Review
- RECODE: a programmable guide-free C-to-U RNA editing tool.Nucleic acids research · 2025Article
- A pentatricopeptide repeat protein restores fertility in Moricandia arvensis based cytoplasmic male sterility system in Brassica juncea.Molecular genetics and genomics : MGG · 2025Article
- Transcriptomic Characterization of Candidate Genes forPathogens (Basel, Switzerland) · 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
- Single-molecule visualization of sequence-specific RNA binding by a designer PPR protein.Nucleic acids research · 2024Article
- Diversity and structural-functional insights of alpha-solenoid proteins.Protein science : a publication of the Protein Society · 2024Review
- Translational activation by a synthetic PPR protein elucidates control of psbA translation in Arabidopsis chloroplasts.The Plant cell · 2024Article
- Applications of Synthetic Pentatricopeptide Repeat Proteins.Plant & cell physiology · 2024Review
- Sls1 and Mtf2 mediate the assembly of the Mrh5C complex required for activation of cox1 mRNA translation.The Journal of biological chemistry · 2024Article
- Discovery, structure, mechanisms, and evolution of protein-only RNase P enzymes.The Journal of biological chemistry · 2024Review
97 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Pentatricopeptide repeat (PPR) proteins are eukaryotic RNA-binding proteins that are commonly found in plants. Organelle transcript processing and stability are mediated by PPR proteins in a gene-specific manner through recognition by tandem arrays of degenerate 35-amino-acid repeating units, the PPR motifs. However, the sequence-specific RNA recognition mechanism of the PPR protein remains largely unknown. Here, we show the principle underlying RNA recognition for PPR proteins involved in RNA editing. The distance between the PPR-RNA alignment and the editable C was shown to be conserved. Amino acid variation at 3 particular positions within the motif determined recognition of a specific RNA in a programmable manner, with a 1-motif to 1-nucleotide correspondence, with no gap sequence. Data from the decoded nucleotide frequencies for these 3 amino acids were used to assign accurate interacting sites to several PPR proteins for RNA editing and to predict the target site for an uncharacterized PPR protein.
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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.