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• W2470378052 abstract "Significance RNA helicases can remodel substrate RNA–protein complexes in diverse ways. However, these activities have typically been studied using noncognate helicase-substrate systems, because the in vivo targets of many helicases are unknown. We investigated how the Brr2 protein disrupts its cognate U4/U6 di-small nuclear RNA–protein complex (di-snRNP), a reaction required for spliceosome catalytic activation. Our results suggest that Brr2 acts like a switch, initiating displacement of U6 snRNA, thereby inducing it to adopt an alternative conformation incompatible with base pairing to U4 snRNA. This mechanism explains how one U4/U6-bound protein, pre-mRNA processing factor 3 (Prp3), is displaced, whereas Prp31 and small nuclear ribonucleoprotein-associated protein 1 (Snu13) are released in complex with U4 snRNA. This unprecedented mode of RNP disruption minimizes requirements for reassembly of the U4/U6 di-snRNP after splicing." @default.
• W2470378052 created "2016-07-22" @default.
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• W2470378052 date "2016-06-27" @default.
• W2470378052 modified "2023-09-27" @default.
• W2470378052 title "Substrate-assisted mechanism of RNP disruption by the spliceosomal Brr2 RNA helicase" @default.
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• W2470378052 doi "https://doi.org/10.1073/pnas.1524616113" @default.
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