ArticleNucleic acids research2014
Quaternary arrangement of an active, native group II intron ribonucleoprotein complex revealed by small-angle X-ray scattering.
Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 16 citations in OpenAlex.
- Organellar Introns in Fungi, Algae, and Plants.Cells · 2021Review
- Exon and protein positioning in a pre-catalytic group II intron RNP primed for splicing.Nucleic acids research · 2020Article
- A group II intron-encoded protein interacts with the cellular replicative machinery through the β-sliding clamp.Nucleic acids research · 2019Article
- Group II Intron RNPs and Reverse Transcriptases: From Retroelements to Research Tools.Cold Spring Harbor perspectives in biology · 2019Review
- Structural accommodations accompanying splicing of a group II intron RNP.Nucleic acids research · 2018Article
- Article
- Reverse transcriptases lend a hand in splicing catalysis.Nature structural & molecular biology · 2016Article
- Structure of a group II intron in complex with its reverse transcriptase.Nature structural & molecular biology · 2016Article
- Functionality ofFrontiers in molecular biosciences · 2016Article
- Emerging applications of small angle solution scattering in structural biology.Protein science : a publication of the Protein Society · 2015Review
- Mobile Bacterial Group II Introns at the Crux of Eukaryotic Evolution.Microbiology spectrum · 2015Review
- Small-angle X-ray scattering: a bridge between RNA secondary structures and three-dimensional topological structures.Current opinion in structural biology · 2015Review
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Authors and funding
9 authors at 4 institutions in 1 country.
Funding
Abstract
The stable ribonucleoprotein (RNP) complex formed between the Lactococcus lactis group II intron and its self-encoded LtrA protein is essential for the intron's genetic mobility. In this study, we report the biochemical, compositional, hydrodynamic and structural properties of active group II intron RNP particles (+A) isolated from its native host using a novel purification scheme. We employed small-angle X-ray scattering to determine the structural properties of these particles as they exist in solution. Using sucrose as a contrasting agent, we derived a two-phase quaternary model of the protein-RNA complex. This approach revealed that the spatial properties of the complex are largely defined by the RNA component, with the protein dimer located near the center of mass. A transfer RNA fusion engineered into domain II of the intron provided a distinct landmark consistent with this interpretation. Comparison of the derived +A RNP shape with that of the previously reported precursor intron (ΔA) particle extends previous findings that the loosely packed precursor RNP undergoes a dramatic conformational change as it compacts into its active form. Our results provide insights into the quaternary arrangement of these RNP complexes in solution, an important step to understanding the transition of the group II intron from the precursor to a species fully active for DNA invasion.
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Registered trials
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