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[摘要]：RNA binding motif protein 5 (RBM5) is a candidate tumor suppressor gene. Recent studies showed that RBM5 functions as an alternative splicing regulator of apoptosis-related genes. Here, we identify DHX15 and PRP19, two spliceosome components, as novel RBM5-interacting partners. We then show that the G-patch domain of RBM5 is indispensable for its ability to interact with DHX15. Strikingly, we find that RBM5 stimulates the helicase activity of DHX15 in a G patch domain-dependent manner in vitro. Helicase activities play critical roles in modulating pre-mRNA splicing. Our findings thus suggest a new mechanism underlying the regulatory roles of RBM5 in pre-mRNA splicing. Structured summary of protein interactions: DHX15 physically interacts with RBM5 by anti tag coimmunoprecipitation (View Interaction: 1, 2, 3, 4, 5, 6, 7). RBM5 binds to PRP19 by pull down (View Interaction: 1, 2) RBM5 binds to DHX15 by pull down (View Interaction: 1, 2) DHX15 physically interacts with RBM5 by two hybrid (View interaction) PRP19 physically interacts with RBM5 by anti tag coimmunoprecipitation (View Interaction: 1, 2) RBM5 binds to U2AF65 by pull down (View interaction) RBM5 physically interacts with DHX15, PRP19, PRPF8 and SNRNP200 by anti tag coimmunoprecipitation (View interaction) RBM5 physically interacts with DHX15, PRP19 and U2AF65 by anti bait coimmunoprecipitation (View interaction) (C) 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. |
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