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首页> 外文期刊>Molecular and Cellular Biology >Assembly of the α-Globin mRNA Stability Complex Reflects Binary Interaction between the Pyrimidine-Rich 3′ Untranslated Region Determinant and Poly(C) Binding Protein αCP
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Assembly of the α-Globin mRNA Stability Complex Reflects Binary Interaction between the Pyrimidine-Rich 3′ Untranslated Region Determinant and Poly(C) Binding Protein αCP

机译：α-球蛋白mRNA稳定复合物的组装反映了嘧啶-富3'非翻译区决定簇和聚（C）结合蛋白αCP之间的二元相互作用

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Globin mRNAs accumulate to 95% of total cellular mRNA during terminal erythroid differentiation, reflecting their extraordinary stability. The stability of human α-globin mRNA is paralleled by formation of a sequence-specific RNA-protein (RNP) complex at a pyrimidine-rich site within its 3′ untranslated region (3′UTR), the α-complex. The proteins of the α-complex are widely expressed. The α-complex or a closely related complex also assembles at pyrimidine-rich 3′UTR segments of other stable mRNAs. These data suggest that the α-complex may constitute a general determinant of mRNA stability. One or more αCPs, members of a family of hnRNP K-homology domain poly(C) binding proteins, are essential constituents of the α-complex. The ability of αCPs to homodimerize and their reported association with additional RNA binding proteins such as AU-rich binding factor 1 (AUF1) and hnRNP K have suggested that the α-complex is a multisubunit structure. In the present study, we have addressed the composition of the α-complex. An RNA titration recruitment assay revealed that αCPs were quantitatively incorporated into the α-complex in the absence of associated AUF1 and hnRNP K. A high-affinity direct interaction between each of the three major αCP isoforms and the α-globin 3′UTR was detected, suggesting that each of these proteins might be sufficient for α-complex assembly. This sufficiency was further supported by the sequence-specific binding of recombinant αCPs to a spectrum of RNA targets. Finally, density sedimentation analysis demonstrated that the α-complex could accommodate only a single αCP. These data established that a single αCP molecule binds directly to the α-globin 3′UTR, resulting in a simple binary structure for the α-complex.
机译：在终末红系分化过程中，globin mRNA累积至细胞总mRNA的95％，反映了它们非凡的稳定性。人α-珠蛋白mRNA的稳定性与在其3'非翻译区（3'UTR）（α-复合物）内富含嘧啶的位点处形成序列特异性RNA-蛋白质（RNP）复合物平行。 α-复合物的蛋白质被广泛表达。 α-复合物或紧密相关的复合物也在其他稳定的mRNA的富含嘧啶的3'UTR区段组装。这些数据表明，α-复合物可以构成mRNA稳定性的一般决定因素。 hnRNP K同源结构域poly（C）结合蛋白家族的一个或多个αCP是α复合体的基本组成部分。 αCPs均二聚的能力及其与其他RNA结合蛋白（例如富AU的结合因子1（AUF1）和hnRNP K）的关联已表明，α-复合物是一个多亚基结构。在本研究中，我们已经解决了α-复合物的组成。 RNA滴定募集试验表明，在没有相关的AUF1和hnRNP K的情况下，αCP被定量地掺入了α-复合物中。检测到三种主要αCP亚型与α-珠蛋白3'UTR之间的高亲和力直接相互作用，表明这些蛋白质中的每一种都可能足以进行α-复合物组装。重组αCP与一系列RNA靶标的序列特异性结合进一步支持了这种充足性。最后，密度沉降分析表明，α-络合物只能容纳一个αCP。这些数据确定了单个αCP分子直接与α-珠蛋白3'UTR结合，从而形成了α-复合物的简单二元结构。

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