ArticleThe Plant cell2006
A pentatricopeptide repeat protein facilitates the trans-splicing of the maize chloroplast rps12 pre-mRNA.
Article in The Plant cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 143 papers.
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143 citing papers in PubMed, 301 citations in OpenAlex.
- The AtRNC1-AtWTF1 protein complex is essential for chloroplast group Ⅱ intron splicing, ribosome biogenesis, and embryo development in Arabidopsis.Plant molecular biology · 2026Article
- Rapid plastid isolation reveals the chloroplast proteome and structures of the chlororibosome large subunit and RuBisCO inbioRxiv : the preprint server for biology · 2026Article
- Pentatricopeptide repeat proteins in crops: Advances in functional mechanisms and breeding applications.Journal of integrative plant biology · 2026Review
- High Conservation of Translation-Enabling RNA Editing Sites in Hyper-editing Ferns Implies They Are Not Selectively Neutral.Molecular biology and evolution · 2025Article
- Experimental evaluation of effectiveness of genomic selection for resistance to northern corn leaf blight in maize.Journal of applied genetics · 2025Article
- P-Type Pentatricopeptide Repeat Proteins YS1 and YS2 Function in Splicing ofInternational journal of molecular sciences · 2025Article
- Barley young leaf chlorina, a putative pentatricopeptide repeat gene, is essential for chloroplast development in young leaves.Plant molecular biology · 2025Article
- Pentatricopeptide repeat proteins in plants: Cellular functions, action mechanisms, and potential applications.Plant communications · 2025Review
- Diversity and structural-functional insights of alpha-solenoid proteins.Protein science : a publication of the Protein Society · 2024Review
- Relevance and regulation of alternative splicing in plant secondary metabolism: current understanding and future directions.Horticulture research · 2024Review
- Identification of candidate gene associated with maize northern leaf blight resistance in a multi-parent population.Plant cell reports · 2024Article
- Applications of Synthetic Pentatricopeptide Repeat Proteins.Plant & cell physiology · 2024Review
- Low-Temperature-Mediated Promoter Methylation Relates to the Expression ofInternational journal of molecular sciences · 2023Article
- Chloroplast gene expression: Recent advances and perspectives.Plant communications · 2023Review
- The Chemical Composition and Transcriptome Analysis Reveal the Mechanism of Color Formation in Tea (International journal of molecular sciences · 2023Article
- Plant organellar RNA maturation.The Plant cell · 2023Review
- A translatome-transcriptome multi-omics gene regulatory network reveals the complicated functional landscape of maize.Genome biology · 2023Article
- Fine mapping of CscpFtsY, a gene conferring the yellow leaf phenotype in cucumber (Cucumis sativus L.).BMC plant biology · 2022Article
- Updated Progress on Group II Intron Splicing Factors in Plant Chloroplasts.Current issues in molecular biology · 2022Review
- An Overview of Pentatricopeptide Repeat (PPR) Proteins in the MossPlants (Basel, Switzerland) · 2022Review
83 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The pentatricopeptide repeat (PPR) is a degenerate 35-amino acid repeat motif that is widely distributed among eukaryotes. Genetic, biochemical, and bioinformatic data suggest that many PPR proteins influence specific posttranscriptional steps in mitochondrial or chloroplast gene expression and that they may typically bind RNA. However, biological functions have been determined for only a few PPR proteins, and with few exceptions, substrate RNAs are unknown. To gain insight into the functions and substrates of the PPR protein family, we characterized the maize (Zea mays) nuclear gene ppr4, which encodes a chloroplast-targeted protein harboring both a PPR tract and an RNA recognition motif. Microarray analysis of RNA that coimmunoprecipitates with PPR4 showed that PPR4 is associated in vivo with the first intron of the plastid rps12 pre-mRNA, a group II intron that is transcribed in segments and spliced in trans. ppr4 mutants were recovered through a reverse-genetic screen and shown to be defective for rps12 trans-splicing. The observations that PPR4 is associated in vivo with rps12-intron 1 and that it is also required for its splicing demonstrate that PPR4 is an rps12 trans-splicing factor. These findings add trans-splicing to the list of RNA-related functions associated with PPR proteins and suggest that plastid group II trans-splicing is performed by different machineries in vascular plants and algae.
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