Tumor suppressor RBM5 directly interacts with the DExD/H-box protein DHX15 and stimulates its helicase activity
Tumor suppressor RBM5 directly interacts with the DExD/H-box protein DHX15 and stimulates its helicase activity
复制标题
DOI：
10.1016/j.febslet.2012.02.052
复制
发表时间：
2012-04-05
期刊：
影响因子：
3.5
通讯作者：
Li, Xialu
中科院分区：
文献类型：
--
作者：
Niu, Zhaoyang;Jin, Wenxing;Li, Xialu
RNA结合基序蛋白5（RBM 5）是一个候选的肿瘤抑制基因。最近的研究表明，RBM 5作为一个选择性剪接调节剂的功能，糖尿病相关基因。在这里，我们确定DHX 15和PRP 19，两个剪接体组件，作为新的RBM 5相互作用的合作伙伴。然后，我们表明RBM 5的G-补丁结构域是必不可少的，其与DHX 15相互作用的能力。引人注目的是，我们发现RBM 5在体外以G补丁结构域依赖性方式刺激DHX 15的解旋酶活性。解旋酶活性在调节前体mRNA剪接中起关键作用。因此，我们的研究结果表明RBM 5在前体mRNA剪接中的调节作用是一种新的机制。蛋白质相互作用的结构性总结：DHX 15通过抗标签免疫共沉淀与RBM 5发生物理相互作用（查看相互作用：1、2、3、4、5、6、7）. RBM 5通过下拉与PRP 19结合（查看交互：1，2）RBM 5通过下拉与DHX 15结合（查看交互：1,2）DHX 15与RBM 5通过两种杂交方式相互作用，（查看相互作用）PRP 19通过抗标签免疫共沉淀与RBM 5发生物理相互作用（查看交互：1，2）RBM 5通过下拉结合U2 AF 65（查看相互作用）RBM 5与DHX 15，PRP 19，PRPF 8和SNRNP 200通过抗标签免疫共沉淀（查看交互）RBM 5与DHX 15物理交互，PRP 19和U2 AF 65通过抗诱饵免疫共沉淀（查看相互作用）（C）2012欧洲生物化学学会联合会。Elsevier B. V.出版，保留所有权利。
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.