Crystallographic studies on molecular motors of the spliceosome (A02)

八种不同的DExD/H-box ATPase促进剪接体的组装、激活和拆卸所需的结构和组成变化。剪接体中Deah-box蛋白Prp2和Prp43的活性分别由与蛋白质Spp2和Ntr1的内在无序G-Patch结构域的直接相互作用特异性地触发，而Prp22显示出高的内在活性。我们旨在揭示G-补丁结构域刺激的结构基础，以及Prp43和Prp22解开RNA的分子机制。

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.