ArticleNucleic acids research2020
Exon and protein positioning in a pre-catalytic group II intron RNP primed for splicing.
Article in Nucleic acids research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 12 citations in OpenAlex.
- Structural Remodeling and Enzymatic Replacement Shape the Evolution of Organellar Group II Introns inInternational journal of molecular sciences · 2026Article
- RNA-Based Therapies for Inherited Metabolic Disorders.Journal of inherited metabolic disease · 2026Review
- Structural basis for the evolution of a domesticated group II intron-like reverse transcriptase to function in host cell DNA repair.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Structural basis of circularly permuted group II intron self-splicing.Nature structural & molecular biology · 2025Article
- Article
- Structures of a mobile intron retroelement poised to attack its structured DNA target.Science (New York, N.Y.) · 2022Article
- Functionalized graphene grids with various charges for single-particle cryo-EM.Nature communications · 2022Article
- Organellar Introns in Fungi, Algae, and Plants.Cells · 2021Review
- Molecular characterization of both transesterification reactions of the group II intron circularization pathway.Nucleic acids research · 2021Article
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
Abstract
Group II introns are the putative progenitors of nuclear spliceosomal introns and use the same two-step splicing pathway. In the cell, the intron RNA forms a ribonucleoprotein (RNP) complex with the intron-encoded protein (IEP), which is essential for splicing. Although structures of spliced group II intron RNAs and RNP complexes have been characterized, structural insights into the splicing process remain enigmatic due to lack of pre-catalytic structural models. Here, we report two cryo-EM structures of endogenously produced group II intron RNPs trapped in their pre-catalytic state. Comparison of the catalytically activated precursor RNP to its previously reported spliced counterpart allowed identification of key structural rearrangements accompanying splicing, including a remodeled active site and engagement of the exons. Importantly, altered RNA-protein interactions were observed upon splicing among the RNP complexes. Furthermore, analysis of the catalytically inert precursor RNP demonstrated the structural impact of the formation of the active site on RNP architecture. Taken together, our results not only fill a gap in understanding the structural basis of IEP-assisted group II intron splicing, but also provide parallels to evolutionarily related spliceosomal splicing.
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Registered trials
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