The multifunctional human p100 protein 'hooks' methylated ligands
The multifunctional human p100 protein 'hooks' methylated ligands
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多功能人类 p100 蛋白“钩住”甲基化配体
DOI：
10.1038/nsmb1269
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发表时间：
2007-08-01
影响因子：
16.8
通讯作者：
Rao, Zihe
中科院分区：
文献类型：
--
作者：
Shaw, Neil;Zhao, Min;Rao, Zihe
人p100蛋白是一种重要的转录调节因子，通过在启动子特异性激活因子和基础转录机制之间形成物理桥梁来增加基因转录。在这里，我们表明，都铎和SN（TSN）域的p100与U小核核糖核蛋白（snRNP）复合物相互作用，这表明在前体信使RNA的加工中的作用p100。我们确定了p100 TSN结构域的晶体结构，以描绘p100的拟议功能的分子基础。叉指结构类似于钩，具有控制钩的移动和取向的铰链。我们的研究表明，一个保守的芳香笼钩甲基snRNP和锚p100的剪接体。这些结构上的见解部分解释了p100在转录和剪接中的独特作用。
The human p100 protein is a vital transcription regulator that increases gene transcription by forming a physical bridge between promoter-specific activators and the basal transcription machinery. Here we demonstrate that the tudor and SN (TSN) domain of p100 interacts with U small nuclear ribonucleoprotein ( snRNP) complexes, suggesting a role for p100 in the processing of precursor messenger RNA. We determined the crystal structure of the p100 TSN domain to delineate the molecular basis of p100's proposed functions. The interdigitated structure resembles a hook, with a hinge controlling the movement and orientation of the hook. Our studies suggest that a conserved aromatic cage hooks methyl groups of snRNPs and anchors p100 to the spliceosome. These structural insights partly explain the distinct roles of p100 in transcription and splicing.