ArticleNucleic acids research2011
The group II intron ribonucleoprotein precursor is a large, loosely packed structure.
Article in Nucleic acids research, 2011. 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.
- The ChloroplastCells · 2021Review
- Exon and protein positioning in a pre-catalytic group II intron RNP primed for splicing.Nucleic acids research · 2020Article
- Structural accommodations accompanying splicing of a group II intron RNP.Nucleic acids research · 2018Article
- Article
- Cryo-EM and the elucidation of new macromolecular structures: Random Conical Tilt revisited.Scientific reports · 2015Article
- Mobile Bacterial Group II Introns at the Crux of Eukaryotic Evolution.Microbiology spectrum · 2015Review
- Quaternary arrangement of an active, native group II intron ribonucleoprotein complex revealed by small-angle X-ray scattering.Nucleic acids research · 2014Article
- Group II intron-ribosome association protects intron RNA from degradation.RNA (New York, N.Y.) · 2013Article
- Telomerase and retrotransposons: reverse transcriptases that shaped genomes.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
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Authors and funding
8 authors.
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Abstract
Group II self-splicing introns are phylogenetically diverse retroelements that are widely held to be the ancestors of spliceosomal introns and retrotransposons that insert into DNA. Folding of group II intron RNA is often guided by an intron-encoded protein to form a catalytically active ribonucleoprotein (RNP) complex that plays a key role in the activity of the intron. To date, possible structural differences between the intron RNP in its precursor and spliced forms remain unexplored. In this work, we have trapped the native Lactococcus lactis group II intron RNP complex in its precursor form, by deleting the adenosine nucleophile that initiates splicing. Sedimentation velocity, size-exclusion chromatography and cryo-electron microscopy provide the first glimpse of the intron RNP precursor as a large, loosely packed structure. The dimensions contrast with those of compact spliced introns, implying that the RNP undergoes a dramatic conformational change to achieve the catalytically active state.
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