Structure of Pumilio reveals similarity between RNA and peptide binding motifs
Structure of Pumilio reveals similarity between RNA and peptide binding motifs
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DOI：
10.1016/s0092-8674(01)00318-x
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发表时间：
2001-04-20
期刊：
影响因子：
64.5
通讯作者：
Aggarwal, AK
中科院分区：
文献类型：
--
作者：
Edwards, TA;Pyle, SE;Aggarwal, AK
翻译调控在动物细胞的分化和发育中起着至关重要的作用。一个被充分研究的案例是在果蝇早期胚胎发生过程中，驼背mRNA受Pumilio、Nanos和Brain Tumor等转录因子的控制。我们在这里报告了一个关键区域的晶体结构，即Puf结构域，它在驼背mRNA的3'非翻译区组织了一个多价抑制复合体。该结构揭示了一个延伸的彩虹形分子，具有串联螺旋重复序列，与β -catenin中的犰狳重复序列和蛋白磷酸酶2A中的HEAT重复序列有着意想不到的相似之处。基于结构和基因实验，我们确定了驼背mRNA及其辅助因子纳米和脑肿瘤的推定相互作用表面。这一分析表明，螺旋重复蛋白的类似特征被用于结合延伸肽和RNA。
Translation regulation plays an essential role in the differentiation and development of animal cells. One well-studied case is the control of hunchback mRNA during early Drosophila embryogenesis by the transacting factors Pumilio, Nanos, and Brain Tumor. We report here a crystal structure of the critical region of Pumilio, the Puf domain, that organizes a multivalent repression complex on the 3' untranslated region of hunchback mRNA. The structure reveals an extended, rainbow shaped molecule, with tandem helical repeats that bear unexpected resemblance to the armadillo repeats in beta -catenin and the HEAT repeats in protein phosphatase 2A. Based on the structure and genetic experiments, we identify putative interaction surfaces for hunchback mRNA and the cofactors Nanos and Brain Tumor. This analysis suggests that similar features in helical repeat proteins are used to bind extended peptides and RNA.