{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["32(5)"],"submitter":["Soni K"],"pubmed_abstract":["Intron removal during pre-mRNA splicing is of extraordinary complexity and its disruption causes a vast number of genetic diseases in humans. While key steps of the canonical spliceosome cycle have been revealed by combined structure-function analyses, structural information on an aberrant spliceosome committed to premature disassembly is not available. Here, we report two cryo-electron microscopy structures of post-B<sup>act</sup> spliceosome intermediates from Schizosaccharomyces pombe primed for disassembly. We identify the DEAH-box helicase-G-patch protein pair (Gih35-Gpl1, homologous to human DHX35-GPATCH1) and show how it maintains catalytic dormancy. In both structures, Gpl1 recognizes a remodeled active site introduced by an overstabilization of the U5 loop I interaction with the 5"],"journal":["Nature structural & molecular biology"],"pagination":["914-925"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12086092"],"repository":["biostudies-literature"],"pubmed_title":["Structures of aberrant spliceosome intermediates on their way to disassembly."],"pmcid":["PMC12086092"],"pubmed_authors":["Dybkov O","Trakansuebkul S","Fischer T","Soni K","Schwan M","Urlaub H","Horvath A","Flemming D","Wild K","Sinning I"],"additional_accession":[]},"is_claimable":false,"name":"Structures of aberrant spliceosome intermediates on their way to disassembly.","description":"Intron removal during pre-mRNA splicing is of extraordinary complexity and its disruption causes a vast number of genetic diseases in humans. While key steps of the canonical spliceosome cycle have been revealed by combined structure-function analyses, structural information on an aberrant spliceosome committed to premature disassembly is not available. Here, we report two cryo-electron microscopy structures of post-B<sup>act</sup> spliceosome intermediates from Schizosaccharomyces pombe primed for disassembly. We identify the DEAH-box helicase-G-patch protein pair (Gih35-Gpl1, homologous to human DHX35-GPATCH1) and show how it maintains catalytic dormancy. In both structures, Gpl1 recognizes a remodeled active site introduced by an overstabilization of the U5 loop I interaction with the 5","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 May","modification":"2026-06-01T06:16:01.727Z","creation":"2026-04-08T09:54:03.051Z"},"accession":"S-EPMC12086092","cross_references":{"pubmed":["39833470"],"doi":["10.1038/s41594-024-01480-7"]}}