作者: Ying Chen , Andreas Boland , Duygu Kuzuoğlu-Öztürk , Praveen Bawankar , Belinda Loh
DOI: 10.1016/J.MOLCEL.2014.03.034
关键词: Genetics 、 Plasma protein binding 、 Protein subunit 、 Biology 、 CCR4-NOT complex 、 Protein structure 、 Cell biology 、 Effector 、 RNA interference 、 Regulation of gene expression 、 Gene silencing
摘要: CCR4-NOT is a major effector complex in miRNA-mediated gene silencing. It recruited to miRNA targets through interactions with tryptophan (W)-containing motifs TNRC6/GW182 proteins and required for both translational repression degradation of targets. Here, we elucidate the structural basis repressive activity its interaction TNRC6/GW182s. We show that conserved CNOT9 subunit attaches domain unknown function (DUF3819) CNOT1 scaffold. The resulting provides binding sites TNRC6/GW182, crystal structure reveals tandem W-binding pockets located CNOT9. further MIF4G interacts C-terminal RecA DDX6, repressor decapping activator. this demonstrates striking similarity eIF4G-eIF4A complex. Together, our data provide missing physical links molecular pathway connects target recognition repression, deadenylation, decapping.