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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Crystal structure of the human ATP-dependent splicing and export factor UAP56.
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Crystal structure of the human ATP-dependent splicing and export factor UAP56.

机译：人类ATP依赖性剪接和输出因子UAP56的晶体结构。

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摘要

Pre-mRNA splicing requires the function of a number of RNA-dependent ATPases/helicases, yet no three-dimensional structure of any spliceosomal ATPases/helicases is known. The highly conserved DECD-box protein UAP56/Sub2 is an essential splicing factor that is also important for mRNA export. The expected ATPase/helicase activity appears to be essential for the UAP56/Sub2 functions. Here, we show that purified human UAP56 is an active RNA-dependent ATPase, and we also report the crystal structures of UAP56 alone and in complex with ADP, as well as a DECD to DEAD mutant. The structures reveal a unique spatial arrangement of the two conserved helicase domains, and ADP-binding induces significant conformational changes of key residues in the ATP-binding pocket. Our structural analyses suggest a specific protein-RNA displacement model of UAP56/Sub2. The detailed structural information provides important mechanistic insights into the splicing function of UAP56/Sub2. The structures also will be useful for the analysis of other spliceosomal DExD-box ATPases/helicases.
机译：mRNA前剪接需要许多RNA依赖性ATPase /螺旋酶的功能，但尚无任何剪接体ATPase /螺旋酶的三维结构已知。高度保守的DECD-box蛋白UAP56 / Sub2是必不可少的剪接因子，对mRNA的输出也很重要。预期的ATPase /解旋酶活性似乎对UAP56 / Sub2功能至关重要。在这里，我们表明纯化的人UAP56是一种活性RNA依赖的ATPase，并且我们还报告了单独和与ADP以及与DEAD到DEAD突变体复合的UAP56的晶体结构。该结构揭示了两个保守的解旋酶结构域的独特空间排列，并且ADP结合诱导ATP结合口袋中关键残基的显着构象变化。我们的结构分析提示了UAP56 / Sub2的特定蛋白质-RNA置换模型。详细的结构信息为UAP56 / Sub2的拼接功能提供了重要的机械见解。该结构还可用于分析其他剪接体DExD-box ATPase /螺旋酶。

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