ArticleThe Plant cell2005
CRS1, a chloroplast group II intron splicing factor, promotes intron folding through specific interactions with two intron domains.
Article in The Plant cell, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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Who cites it
50 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
- Plant mitochondrial PORR proteins facilitate group II intron splicing by binding to distinct regions within their target introns.Nucleic acids research · 2025Article
- The RiceBiology · 2024Article
- GhCTSF1, a short PPR protein with a conserved role in chloroplast development and photosynthesis, participates in intron splicing of rpoC1 and ycf3-2 transcripts in cotton.Plant communications · 2024Article
- Plant organellar RNA maturation.The Plant cell · 2023Review
- Updated Progress on Group II Intron Splicing Factors in Plant Chloroplasts.Current issues in molecular biology · 2022Review
- An overview of RNA splicing and functioning of splicing factors in land plant chloroplasts.RNA biology · 2022Article
- Development of an In Vitro Chloroplast Splicing System: Sequences Required for Correct pre-mRNA Splicing.Plant & cell physiology · 2021Article
- An Exon Skipping inInternational journal of molecular sciences · 2021Article
- The ChloroplastCells · 2021Review
- Regulator of Chromosome Condensation 1-Domain Protein DEK47 Functions on the Intron Splicing of MitochondrialFrontiers in plant science · 2021Article
- OsCAF2 contains two CRM domains and is necessary for chloroplast development in rice.BMC plant biology · 2020Article
- The bRPS6-Family Protein RFC3 Prevents Interference by the Splicing Factor CFM3b during Plastid rRNA Biogenesis inPlants (Basel, Switzerland) · 2020Article
- Characterization of the CRM Gene Family and Elucidating the Function of OsCFM2 in Rice.Biomolecules · 2020Article
- Article
- The dual-targeted RNA editing factor AEF1 is universally conserved among angiosperms and reveals only minor adaptations upon loss of its chloroplast or its mitochondrial target.Plant molecular biology · 2020Article
- PUMPKIN, the Sole Plastid UMP Kinase, Associates with Group II Introns and Alters Their Metabolism.Plant physiology · 2019Article
- Comparative assessment of chloroplast transcriptional responses highlights conserved and unique patterns across Triticeae members under salt stress.Photosynthesis research · 2018Article
- OsPPR6, a pentatricopeptide repeat protein involved in editing and splicing chloroplast RNA, is required for chloroplast biogenesis in rice.Plant molecular biology · 2017Article
- The Reverse Transcriptase/RNA Maturase Protein MatR Is Required for the Splicing of Various Group II Introns in Brassicaceae Mitochondria.The Plant cell · 2016Article
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4 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Group II introns are ribozymes that catalyze a splicing reaction with the same chemical steps as spliceosome-mediated splicing. Many group II introns have lost the capacity to self-splice while acquiring compensatory interactions with host-derived protein cofactors. Degenerate group II introns are particularly abundant in the organellar genomes of plants, where their requirement for nuclear-encoded splicing factors provides a means for the integration of nuclear and organellar functions. We present a biochemical analysis of the interactions between a nuclear-encoded group II splicing factor and its chloroplast intron target. The maize (Zea mays) protein Chloroplast RNA Splicing 1 (CRS1) is required specifically for the splicing of the group II intron in the chloroplast atpF gene and belongs to a plant-specific protein family defined by a recently recognized RNA binding domain, the CRM domain. We show that CRS1's specificity for the atpF intron in vivo can be explained by CRS1's intrinsic RNA binding properties. CRS1 binds in vitro with high affinity and specificity to atpF intron RNA and does so through the recognition of elements in intron domains I and IV. These binding sites are not conserved in other group II introns, accounting for CRS1's intron specificity. In the absence of CRS1, the atpF intron has little uniform tertiary structure even at elevated [Mg2+]. CRS1 binding reorganizes the RNA, such that intron elements expected to be at the catalytic core become less accessible to solvent. We conclude that CRS1 promotes the folding of its group II intron target through tight and specific interactions with two peripheral intron segments.
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