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首页> 外文期刊>Journal of Molecular Biology >Structural analysis of the quaking homodimerization interface
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Structural analysis of the quaking homodimerization interface

机译：地震均二聚化界面的结构分析

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摘要

Quaking (QkI) is a prototypical member of the STAR (signal transducer and activator of RNA) protein family, which plays key roles in posttranscriptional gene regulation by controlling mRNA translation, stability and splicing. QkI-5 has been shown to regulate mRNA expression in the central nervous system, but little is known about its roles in other tissues. STAR proteins function as dimers and bind to bipartite RNA sequences; however, the structural and functional roles of homodimerization and heterodimerization are still unclear. Here, we present the crystal structure of the QkI dimerization domain, which adopts a similar stacked helix-turn-helix arrangement as its homologs GLD-1 (germ line development defective-1) and Sam68 (Src-associated protein during mitosis, 68 kDa) but differs by an additional helix inserted in the dimer interface. Variability of the dimer interface residues likely ensures selective homodimerization by preventing association with non-cognate STAR family proteins in the cell. Mutations that inhibit dimerization also significantly impair RNA binding in vitro, alter QkI-5 protein levels and impair QkI function in a splicing assay in vivo. Together, our results indicate that a functional Qua1 homodimerization domain is required for QkI-5 function in mammalian cells.
机译：Quaking（QkI）是STAR（信号转导和RNA激活剂）蛋白家族的典型成员，它通过控制mRNA的翻译，稳定性和剪接在转录后基因调控中发挥关键作用。 QkI-5已被证明可调节中枢神经系统中的mRNA表达，但对其在其他组织中的作用知之甚少。 STAR蛋白起二聚体的作用并与二分体RNA序列结合;然而，均二聚和异二聚的结构和功能作用仍不清楚。在这里，我们介绍QkI二聚结构域的晶体结构，该结构采用类似的堆积螺旋-转-螺旋排列，作为其同源物GLD-1（胚系发育缺陷-1）和Sam68（有丝分裂期间Src相关蛋白，68 kDa） ），但在二聚体界面中插入了一个额外的螺旋线。二聚体界面残基的可变性可能通过防止与细胞中非同源STAR家族蛋白缔合而确保选择性均二聚。在体内剪接测定中，抑制二聚化的突变还显着损害体外RNA结合，改变QkI-5蛋白水平并损害QkI功能。在一起，我们的结果表明，在哺乳动物细胞中QkI-5功能需要功能性Qua1同型二聚结构域。

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