Department of Molecular and Cell Biology, University of California, Berkeley, California, USA.
Nat Struct Mol Biol. 2010 Feb;17(2):238-40. doi: 10.1038/nsmb.1768. Epub 2010 Jan 24.
GW182-family proteins are essential for microRNA-mediated translational repression and deadenylation in animal cells. Here we show that a conserved motif in the human GW182 paralog TNRC6C interacts with the C-terminal domain of polyadenylate binding protein 1 (PABC) and present the crystal structure of the complex. Mutations at the complex interface impair mRNA deadenylation in mammalian cell extracts, suggesting that the GW182-PABC interaction contributes to microRNA-mediated gene silencing.
GW182 家族蛋白对于动物细胞中 microRNA 介导的翻译抑制和脱腺苷酸化是必需的。在这里，我们显示人类 GW182 同源物 TNRC6C 中的一个保守基序与多聚腺苷酸结合蛋白 1 (PABC) 的 C 末端结构域相互作用，并呈现复合物的晶体结构。在复合物界面处的突变会损害哺乳动物细胞提取物中的 mRNA 脱腺苷酸化，表明 GW182-PABC 相互作用有助于 microRNA 介导的基因沉默。
