The structure of the CstF-77 homodimer provides insights into CstF assembly.
The structure of the CstF-77 homodimer provides insights into CstF assembly.
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DOI：
10.1093/nar/gkm458
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发表时间：
2007
影响因子：
14.9
通讯作者：
Fribourg, Sebastien
中科院分区：
文献类型：
--
作者：
Legrand, Pierre;Pinaud, Noel;Minvielle-Sebastia, Lionel;Fribourg, Sebastien
裂解刺激因子（CstF）是mrna 3′端poly(A)尾形成的第一步。这种异三聚体复合物围绕77-kDa蛋白构建，连接CstF-64和CstF-50亚基。我们已经以2 Å的分辨率解算出了来自cuniculi Encephalitozoon的77-kDa蛋白的晶体结构。该结构围绕11个Half-a-TPR重复折叠，定义了两个结构域。晶体结构揭示了一个紧密的同型二聚体，暴露了与蛋白质伴侣相互作用的系统发育保守区域。定位实验发现，酵母CstF-77的对应物Rna14p的c端区域是酵母CstF-64的同源物Rna15p的对接域。
The cleavage stimulation factor (CstF) is essential for the first step of poly(A) tail formation at the 3' ends of mRNAs. This heterotrimeric complex is built around the 77-kDa protein bridging both CstF-64 and CstF-50 subunits. We have solved the crystal structure of the 77-kDa protein from Encephalitozoon cuniculi at a resolution of 2 Å. The structure folds around 11 Half-a-TPR repeats defining two domains. The crystal structure reveals a tight homodimer exposing phylogenetically conserved areas for interaction with protein partners. Mapping experiments identify the C-terminal region of Rna14p, the yeast counterpart of CstF-77, as the docking domain for Rna15p, the yeast CstF-64 homologue.