Institut Européen de Chimie et Biologie, Institut National de la Santé et de la Recherche Médicale (INSERM) U869, Pessac, France.
RNA. 2011 Mar;17(3):412-8. doi: 10.1261/rna.2481011. Epub 2011 Jan 13.
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.
剪接刺激因子(CstF)复合物由三个亚基组成,是前体 mRNA 3'-端加工所必需的。CstF 识别 U 和 U/G 丰富的顺式作用 RNA 序列元件,并帮助稳定切割和多聚腺苷酸化特异性因子(CPSF)在多聚腺苷酸化位点,以进行有效的 RNA 切割。在这里,我们描述了果蝇 CstF-50 亚基的 N 端结构域的晶体结构。它形成一个紧凑的同源二聚体,暴露两个几何上相反的、相同的和保守的表面,可能作为结合平台。与 CstF-77 结构的先前数据一起,CstF-50 N 端结构域的同源二聚化支持 CstF 的功能状态是异六聚体的模型。