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

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. © 2020, Schuller et al.

Citation

Sandra K Schuller, Jan M Schuller, J Rajan Prabu, Marc Baumgärtner, Fabien Bonneau, Jérôme Basquin, Elena Conti. Structural insights into the nucleic acid remodeling mechanisms of the yeast THO-Sub2 complex. eLife. 2020 Nov 16;9

Mesh Tags

Substances

PMID: 33191913

search → result