%0 Journal Article %T The G-patch activators Pfa1 and PINX1 exhibit different modes of interaction with the Prp43 RNA helicase %+ Laboratoire des Interactions Plantes Microbes Environnement (LIPME) %+ Centre de Biologie Intégrative (CBI) %A Mouffok, Saïda %A Capeyrou, Régine %A Belhabich-Baumas, Kamila %A Joret, Clément %A Henras, Anthony %A Humbert, Odile %A Henry, Yves %Z Ministere de l'Enseignement Superieur et de la Recherche %Z Ligue Contre le Cancer (equipe labellisee) %< avec comité de lecture %@ 1547-6286 %J RNA Biology %I Taylor & Francis %V 18 %N 4 %P 510-522 %8 2021-04-03 %D 2021 %R 10.1080/15476286.2020.1818458 %M 32882145 %K RNA helicase %K ATPase %K G-patch protein %K OB fold %K ribosome synthesis %Z Life Sciences [q-bio]/Biochemistry, Molecular Biology %Z Life Sciences [q-bio]/Cellular Biology/Cell Behavior [q-bio.CB] %Z Life Sciences [q-bio]/Biochemistry, Molecular Biology/Genomics [q-bio.GN]Journal articles %X 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. %G English %Z Estonian Research Council %2 https://cnrs.hal.science/hal-03070370/document %2 https://cnrs.hal.science/hal-03070370/file/Sa%C3%AFda%20MOUFFOK%20et%20al.pdf %L hal-03070370 %U https://cnrs.hal.science/hal-03070370 %~ UNIV-TLSE3 %~ CNRS %~ INRAE %~ ANR %~ INRAEOCCITANIETOULOUSE %~ UNIV-UT3 %~ UT3-INP %~ UT3-TOULOUSEINP %~ LIPME