Crystallographic studies on molecular motors of the spliceosome (A02)

剪接体分子马达的晶体学研究（A02）

• 批准号: 174570643
• 金额: --
• 依托单位: Abteilung für Molekulare Strukturbiologie
• 依托单位国家: 德国
• 项目类别: Collaborative Research Centres
• 财政年份: 2010
• 资助国家: 德国
• 起止时间: 2009-12-31 至 2021-12-31
• 项目状态: 已结题
• 来源: https://gepris.dfg.de/gepris/projekt/174570643?language=en
• 关键词: Crystallographic; studies; molecular; motors; spliceosome

Eight different DExD/H-box ATPases promote the structural and compositional changes required for the assembly, activation and disassembly of the spliceosome. The activities of the DEAH-box proteins Prp2 and Prp43 in the spliceosome are specifically triggered by direct interaction with the intrinsically disordered G-patch domains of the proteins Spp2 and Ntr1, respectively, while Prp22 exhibits a high intrinsic activity. We aim to unravel the structural basis for the stimulation by G-patch domains, as well as the molecular mechanism of RNA unwinding by Prp43 and Prp22.

八种不同的 DExD/H-box ATP 酶促进剪接体组装、激活和分解所需的结构和组成变化。剪接体中 DEAH-box 蛋白 Prp2 和 Prp43 的活性是通过分别与蛋白质 Spp2 和 Ntr1 的本质无序 G 补丁结构域直接相互作用而特异性触发的，而 Prp22 表现出高内在活性。我们的目标是揭示 G-patch 结构域刺激的结构基础，以及 Prp43 和 Prp22 RNA 解旋的分子机制。