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Yeast Prp2 liberates the 5′ splice site and the branch site adenosine for catalysis of pre-mRNA splicing

dc.contributor.authorBao, Penghui
dc.contributor.authorHöbartner, Claudia
dc.contributor.authorHartmuth, Klaus
dc.contributor.authorLührmann, Reinhard
dc.date.accessioned2019-12-17T10:25:22Z
dc.date.available2019-12-17T10:25:22Z
dc.date.issued2017de
dc.relation.ISSN1469-9001de
dc.identifier.urihttp://resolver.sub.uni-goettingen.de/purl?gs-1/16996
dc.description.abstractThe RNA helicase Prp2 facilitates the remodeling of the spliceosomal Bact complex to the catalytically activated B* complex just before step one of splicing. As a high-resolution cryo-EM structure of the B* complex is currently lacking, the precise spliceosome remodeling events mediated by Prp2 remain poorly understood. To investigate the latter, we used chemical structure probing to compare the RNA structure of purified yeast Bact and B* complexes. Our studies reveal deviations from conventional RNA helices in the functionally important U6 snRNA internal stem-loop and U2/U6 helix Ib in the activated Bact complex, and to a lesser extent in B*. Interestingly, the N7 of U6-G60 of the catalytic triad becomes accessible to DMS modification in the B* complex, suggesting that the Hoogsteen interaction with U6-A52 is destabilized in B*. Our data show that Prp2 action does not unwind double-stranded RNA, but enhances the flexibility of the first step reactants, the pre-mRNA's 5' splice site and branch site adenosine. Prp2 therefore appears to act primarily as an RNPase to achieve catalytic activation by liberating the first step reactants in preparation for catalysis of the first step of splicing.de
dc.language.isoengde
dc.rightsopenAccess
dc.rights.urihttps://creativecommons.org/licenses/by-nc/4.0/
dc.subjectPrp2 RNA helicase; RNA structure; activated spliceosome; catalytic activationde
dc.subject.ddc540
dc.titleYeast Prp2 liberates the 5′ splice site and the branch site adenosine for catalysis of pre-mRNA splicingde
dc.typejournalArticlede
dc.identifier.doi10.1261/rna.063115.117
dc.type.versionpublishedVersionde
dc.relation.pISSN1355-8382
dc.relation.eISSN1469-9001
dc.bibliographicCitation.volume23de
dc.bibliographicCitation.issue12de
dc.bibliographicCitation.firstPage1770de
dc.bibliographicCitation.lastPage1779de
dc.type.subtypejournalArticle
dc.identifier.pmid28864812
dc.description.statuspeerReviewedde
dc.bibliographicCitation.journalRNAde


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