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Journal article
Visualizing group II intron dynamics between the first and second steps of splicing
Nature communications, Vol.11(1), pp.2837-2837
05 Jun 2020
PMID: 32503992
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
Group II introns are ubiquitous self-splicing ribozymes and retrotransposable elements evolutionarily and chemically related to the eukaryotic spliceosome, with potential applications as gene-editing tools. Recent biochemical and structural data have captured the intron in multiple conformations at different stages of catalysis. Here, we employ enzymatic assays, X-ray crystallography, and molecular simulations to resolve the spatiotemporal location and function of conformational changes occurring between the first and the second step of splicing. We show that the first residue of the highly-conserved catalytic triad is protonated upon 5'-splice-site scission, promoting a reversible structural rearrangement of the active site (toggling). Protonation and active site dynamics induced by the first step of splicing facilitate the progression to the second step. Our insights into the mechanism of group II intron splicing parallels functional data on the spliceosome, thus reinforcing the notion that these evolutionarily-related molecular machines share the same enzymatic strategy.
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Details
- Title
- Visualizing group II intron dynamics between the first and second steps of splicing
- Creators
- Jacopo Manigrasso - Italian Institute of TechnologyIsabel Chillón - European Molecular Biology LaboratoryVito Genna - Institute for Research in BiomedicinePietro Vidossich - Italian Institute of TechnologySrinivas Somarowthu - Drexel UniversityAnna Marie Pyle - Yale UniversityMarco De Vivo - Italian Institute of TechnologyMarco Marcia - European Molecular Biology LaboratoryArgonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
- Publication Details
- Nature communications, Vol.11(1), pp.2837-2837
- Publisher
- Springer Nature
- Grant note
- P30 GM124165 / NIGMS NIH HHS Howard Hughes Medical Institute S10 OD021527 / NIH HHS
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Biochemistry and Molecular Biology
- Identifiers
- 991019167457204721
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- Domestic collaboration
- International collaboration
- Web of Science research areas
- Biochemistry & Molecular Biology