Structure and assembly of the NOT10:11 module of the CCR4-NOT complex

被引：0

作者：

Levdansky, Yevgen ^{[1
]}

Raisch, Tobias ^{[2
]}

Deme, Justin C. ^{[3
]}

Pekovic, Filip ^{[1
]}

Elmlund, Hans ^{[3
]}

Lea, Susan M. ^{[3
]}

Valkov, Eugene ^{[1
,3
]}

机构：

[1] NCI, Ctr Canc Res, RNA Biol Lab, Frederick, MD 21702 USA

[2] Max Planck Inst Mol Physiol, Dept Struct Biochem, Dortmund, Germany

[3] NCI, Ctr Struct Biol, Ctr Canc Res, Frederick, MD 21702 USA

来源：

COMMUNICATIONS BIOLOGY | 2023年 / 6卷 / 01期

基金：

美国国家卫生研究院;

关键词：

DEADENYLASE COMPLEX; DEGRADATION;

D O I：

10.1038/s42003-023-05122-4

中图分类号：

Q [生物科学];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

NOT1, NOT10, and NOT11 form a conserved module in the CCR4-NOT complex, critical for post-transcriptional regulation in eukaryotes, but how this module contributes to the functions of the CCR4-NOT remains poorly understood. Here, we present cryo-EM structures of human and chicken NOT1:NOT10:NOT11 ternary complexes to sub-3 & ANGS; resolution, revealing an evolutionarily conserved, flexible structure. Through biochemical dissection studies, which include the Drosophila orthologs, we show that the module assembly is hierarchical, with NOT11 binding to NOT10, which then organizes it for binding to NOT1. A short proline-rich motif in NOT11 stabilizes the entire module assembly. Structural and biochemical characterization of the human, chicken, and Drosophila NOT1:NOT10:NOT11 ternary complexes reveal the evolutionarily conserved NOT10:11 module, hierarchical assembly of the complex.

引用

页数：8