Structural insights into the nucleic acid remodeling mechanisms of the yeast THO-Sub2 complex

eLife

Fabien Bonneau¹  Sandra K Schuller¹  Jan M Schuller¹  J Rajan Prabu¹  Elena Conti¹  Jérôme Basquin¹  Marc Baumgärtner¹ 

[1] Department of Structural Cell Biology, Max Planck Institute of Biochemistry, Munich, Germany;

关键词: RNA;    helicase;    R-loops;    CryoEM;    RNA export;    transcription;   

DOI  :  10.7554/eLife.61467

来源: DOAJ

【 摘 要 】

The yeast THO complex is recruited to active genes and interacts with the RNA-dependent ATPase Sub2 to facilitate the formation of mature export-competent messenger ribonucleoprotein particles and to prevent the co-transcriptional formation of RNA:DNA-hybrid-containing structures. How THO-containing complexes function at the mechanistic level is unclear. Here, we elucidated a 3.4 Å resolution structure of Saccharomyces cerevisiae THO-Sub2 by cryo-electron microscopy. THO subunits Tho2 and Hpr1 intertwine to form a platform that is bound by Mft1, Thp2, and Tex1. The resulting complex homodimerizes in an asymmetric fashion, with a Sub2 molecule attached to each protomer. The homodimerization interfaces serve as a fulcrum for a seesaw-like movement concomitant with conformational changes of the Sub2 ATPase. The overall structural architecture and topology suggest the molecular mechanisms of nucleic acid remodeling during mRNA biogenesis.

【 授权许可】

Unknown