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- W1997403103 endingPage "2946" @default.
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- W1997403103 abstract "The elaborate and energy-intensive spliceosome assembly pathway belies the seemingly simple chemistry of pre-mRNA splicing. Prp38p was previously identified as a protein required in vivo and in vitro for the first pre-mRNA cleavage reaction catalyzed by the spliceosome. Here we show that Prp38p is a unique component of the U4/U6.U5 tri-small nuclear ribonucleoprotein (snRNP) particle and is necessary for an essential step late in spliceosome maturation. Without Prp38p activity spliceosomes form, but arrest in a catalytically impaired state. Functional spliceosomes shed U4 snRNA before 5' splice-site cleavage. In contrast, Prp38p-defective spliceosomes retain U4 snRNA bound to its U6 snRNA base-pairing partner. Prp38p is the first tri-snRNP-specific protein shown to be dispensable for assembly, but required for conformational changes which lead to catalytic activation of the spliceosome." @default.
- W1997403103 created "2016-06-24" @default.
- W1997403103 creator A5084307208 @default.
- W1997403103 date "1998-05-15" @default.
- W1997403103 modified "2023-10-01" @default.
- W1997403103 title "Progression through the spliceosome cycle requires Prp38p function for U4/U6 snRNA dissociation" @default.
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- W1997403103 doi "https://doi.org/10.1093/emboj/17.10.2938" @default.
- W1997403103 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1170634" @default.
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