ArticleNature communications2016
Structural basis for specific single-stranded RNA recognition by designer pentatricopeptide repeat proteins.
Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 93 papers.
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Who cites it
93 citing papers in PubMed.
- PPR9 mediates mitochondrial nad transcript maturation required for complex I biogenesis and early plant development in Arabidopsis.Plant molecular biology · 2026Article
- Uncovering the role of the PPR protein PHOTOSYSTEM ONE BIOGENESIS FACTOR6 in splicing chloroplast group II introns.Journal of integrative plant biology · 2026Article
- Pentatricopeptide repeat proteins in crops: Advances in functional mechanisms and breeding applications.Journal of integrative plant biology · 2026Review
- 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
- A Generalized AI View of Tricopeptide Repeats: What's in a Name.International journal of molecular sciences · 2025Review
- FASTK post-transcriptional regulators - a 'FAST-tracK' in mitochondrial gene expression.Biochemical Society transactions · 2025Review
- GRASP: a modular toolkit for building synthetic pentatricopeptide repeat RNA-binding proteins.Nucleic acids research · 2025Article
- Insights into the translational activation mechanisms of the COX1 mRNA in yeast mitochondria.Journal of cell science · 2025Article
- De novo RNA base editing in plant organelles with engineered synthetic P-type PPR editing factors.Nucleic acids research · 2025Article
- Pentatricopeptide repeat proteins in plants: Cellular functions, action mechanisms, and potential applications.Plant communications · 2025Review
- Targeted introduction of premature stop codon in plant mitochondrial mRNA by a designer pentatricopeptide repeat protein with C-to-U editing function.The Plant journal : for cell and molecular biology · 2025Article
- 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
- Single-molecule visualization of sequence-specific RNA binding by a designer PPR protein.Nucleic acids research · 2024Article
- GENOMES UNCOUPLED PROTEIN1 binds to plastid RNAs and promotes their maturation.Plant communications · 2024Article
- Sequence-dependent conformational preferences of disordered single-stranded RNA.Cell reports. Physical science · 2024Article
- 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
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33 more citing papers are in PubMed but not listed here.
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Authors and funding
12 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
As a large family of RNA-binding proteins, pentatricopeptide repeat (PPR) proteins mediate multiple aspects of RNA metabolism in eukaryotes. Binding to their target single-stranded RNAs (ssRNAs) in a modular and base-specific fashion, PPR proteins can serve as designable modules for gene manipulation. However, the structural basis for nucleotide-specific recognition by designer PPR (dPPR) proteins remains to be elucidated. Here, we report four crystal structures of dPPR proteins in complex with their respective ssRNA targets. The dPPR repeats are assembled into a right-handed superhelical spiral shell that embraces the ssRNA. Interactions between different PPR codes and RNA bases are observed at the atomic level, revealing the molecular basis for the modular and specific recognition patterns of the RNA bases U, C, A and G. These structures not only provide insights into the functional study of PPR proteins but also open a path towards the potential design of synthetic sequence-specific RNA-binding proteins.
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