Hexameric architecture of CstF supported by CstF-50 homodimerization domain structure
Hexameric architecture of CstF supported by CstF-50 homodimerization domain structure
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DOI：
10.1261/rna.2481011
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发表时间：
2011-03-01
期刊：
影响因子：
4.5
通讯作者：
Fribourg, Sebastien
中科院分区：
文献类型：
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作者：
Moreno-Morcillo, Maria;Minvielle-Sebastia, Lionel;Fribourg, Sebastien
切割刺激因子（CstF）复合物由三个亚基组成，并且对于前mRNA 3 '端加工是必需的。CstF识别富含U和G/U的顺式作用RNA序列元件，并有助于稳定多聚腺苷酸化位点处的切割和多聚腺苷酸化特异性因子（CPSF），这是生产性RNA切割所需的。在这里，我们描述了果蝇CstF-50亚基的N-末端结构域的晶体结构。它形成紧凑的同源二聚体，暴露出两个几何上相反的、相同的和保守的表面，可以用作结合平台。与先前的数据CstF-77的结构，同源二聚化的CstF-50 N-末端结构域支持的模型，其中CstF的功能状态是一个异源六聚体。
The Cleavage stimulation Factor (CstF) complex is composed of three subunits and is essential for pre-mRNA 3'-end processing. CstF recognizes U and G/U-rich cis-acting RNA sequence elements and helps stabilize the Cleavage and Polyadenylation Specificity Factor (CPSF) at the polyadenylation site as required for productive RNA cleavage. Here, we describe the crystal structure of the N-terminal domain of Drosophila CstF-50 subunit. It forms a compact homodimer that exposes two geometrically opposite, identical, and conserved surfaces that may serve as binding platform. Together with previous data on the structure of CstF-77, homodimerization of CstF-50 N-terminal domain supports the model in which the functional state of CstF is a heterohexamer.