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The G-patch activators Pfa1 and PINX1 exhibit different modes of interaction with the Prp43 RNA helicase

Abstract : Prp43 is a DEAH-box RNA helicase involved in both splicing and ribosome biogenesis. Its activities are directly stimulated by several co-activators that share a G-patch domain. The substrates of Prp43, its mechanism of action and the modes of interaction with and activation by G-patch proteins have been only partially characterized. We investigated how Pfa1 and PINX1, two G-patch proteins involved in ribosome biogenesis, interact with Prp43. We demonstrate that a protruding loop connecting the β4 and β5 strands of Prp43 OB fold is crucial for the binding of the G-patch domain of Pfa1. However, neither this loop nor the entire OB fold of Prp43 is essential for PINX1 binding. We conclude that the binding modes of Pfa1 and PINX1 G-patches to Prp43 are different. Nevertheless, stimulation of the ATPase and helicase activities of Prp43 by both full-length Pfa1 and PINX1 requires the β4-β5 loop. Moreover, we show that disruption of this loop completely abrogates Prp43 activity during yeast ribosome biogenesis but does not prevent its integration within pre-ribosomal particles. We propose that the β4-β5 loop plays a crucial role in the transmission of conformational changes induced by binding of the G-patch to Prp43 active site and substrate RNA.
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Submitted on : Tuesday, December 15, 2020 - 6:18:40 PM
Last modification on : Thursday, July 21, 2022 - 2:29:41 PM
Long-term archiving on: : Tuesday, March 16, 2021 - 8:17:25 PM


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Saïda Mouffok, Régine Capeyrou, Kamila Belhabich-Baumas, Clément Joret, Anthony Henras, et al.. The G-patch activators Pfa1 and PINX1 exhibit different modes of interaction with the Prp43 RNA helicase. RNA Biology, Taylor & Francis, 2021, 18 (4), pp.510-522. ⟨10.1080/15476286.2020.1818458⟩. ⟨hal-03070370⟩



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