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• W2912940165 endingPage "714" @default.
• W2912940165 startingPage "710" @default.
• W2912940165 abstract "During exon ligation, the Saccharomyces cerevisiae spliceosome recognizes the 3'-splice site (3'SS) of precursor messenger RNA (pre-mRNA) through non-Watson-Crick pairing with the 5'SS and the branch adenosine, in a conformation stabilized by Prp18 and Prp8. Here we present the 3.3-angstrom cryo-electron microscopy structure of a human postcatalytic spliceosome just after exon ligation. The 3'SS docks at the active site through conserved RNA interactions in the absence of Prp18. Unexpectedly, the metazoan-specific FAM32A directly bridges the 5'-exon and intron 3'SS of pre-mRNA and promotes exon ligation, as shown by functional assays. CACTIN, SDE2, and NKAP-factors implicated in alternative splicing-further stabilize the catalytic conformation of the spliceosome during exon ligation. Together these four proteins act as exon ligation factors. Our study reveals how the human spliceosome has co-opted additional proteins to modulate a conserved RNA-based mechanism for 3'SS selection and to potentially fine-tune alternative splicing at the exon ligation stage." @default.
• W2912940165 created "2019-02-21" @default.
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• W2912940165 date "2019-02-15" @default.
• W2912940165 modified "2023-10-18" @default.
• W2912940165 title "A human postcatalytic spliceosome structure reveals essential roles of metazoan factors for exon ligation" @default.
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• W2912940165 doi "https://doi.org/10.1126/science.aaw5569" @default.
• W2912940165 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6386133" @default.
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• W2912940165 hasPublicationYear "2019" @default.
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