ArticleProceedings of the National Academy of Sciences of the United States of America2026
Controlled dynamic remodeling of the spliceosome active site enables the first step of splicing.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed.
- Atomistic Simulations Decode the Mechanisms of DNA and RNA Processing Enzymes: Function through Motion.Accounts of chemical research · 2026Article
- Controlled dynamic remodeling of the spliceosome active site enables the first step of splicing.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
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5 authors.
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Abstract
Recent cryoelectron microscopy data have revealed significant conformational rearrangements of the megadalton spliceosome structure during splicing, an essential catalytic process for maturing most human transcripts. However, the molecular trigger of these structural rearrangements for splicing catalysis remains unclear at the atomic level. Here, by analyzing a consistent dataset of multicomponent spliceosome structures, we identified a minimal set of positively charged residues whose dynamic action remodels the spliceosome active site during the first step of splicing. Through equilibrium and enhanced sampling molecular dynamics simulations of multiple splicing intermediates (>2M atoms), we uncover how these residues dynamically operate in coordination with the transient, temporally ordered binding of key spliceosomal proteins (Prp11, Prp8, and Yju2) at the spliceosome core. Our findings reveal a molecular mechanism that ensures precise and timely spliceosome activation, opening promising directions to probe splicing regulation and potentially target its dysfunction in diseases, with broad implications for drug discovery and medicine.
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