Legrand Pierre, Pinaud Noël, Minvielle-Sébastia Lionel, Fribourg Sébastien
Institut Européen de Chimie et Biologie, INSERM U869, 2 rue Robert Escarpit Pessac, F-33607, Université Victor Segalen, Bordeaux 2.
Nucleic Acids Res. 2007;35(13):4515-22. doi: 10.1093/nar/gkm458. Epub 2007 Jun 21.
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 A. 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.
切割刺激因子（CstF）对于mRNA 3'端聚腺苷酸（poly(A)）尾巴形成的第一步至关重要。这种异源三聚体复合物围绕着77 kDa的蛋白质构建，该蛋白质连接CstF-64和CstF-50两个亚基。我们已解析了来自微小隐孢子虫的77 kDa蛋白质的晶体结构，分辨率为2 Å。该结构围绕11个半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，其暴露了用于与蛋白质伙伴相互作用的系统发育保守区域。定位实验确定了CstF-77在酵母中的对应物Rna14p的C末端区域，作为酵母CstF-64同源物Rna15p的对接结构域。
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