7APX

yeast THO-Sub2 complex

Summary for 7APX

• Entry DOI: 10.2210/pdb7apx/pdb
• EMDB information: 11859
• Descriptor: THO complex subunit 2,Tho2, THO complex subunit HPR1, THO complex subunit THP2, ... (6 entities in total)
• Functional Keywords: yeast tho complex s. cerevisiae tho-sub2 the transcription-export (trex) complex, rna binding protein
• Biological source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast); More
• Total number of polymer chains: 6
• Total formula weight: 433842.59

Authors

Schuller, S.K.,Schuller, J.M.,Prabu, R.J.,Baumgartner, M.,Bonneau, F.,basquin, J.,Conti, E. (deposition date: 2020-10-20, release date: 2020-12-02, Last modification date: 2024-05-01)

Primary citation

Schuller, S.K.,Schuller, J.M.,Prabu, J.R.,Baumgartner, M.,Bonneau, F.,Basquin, J.,Conti, E.
Structural insights into the nucleic acid remodeling mechanisms of the yeast THO-Sub2 complex.
Elife, 9:-, 2020

PubMed Abstract: 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 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.

PubMed: 33191913
DOI: 10.7554/eLife.61467

Experimental method

ELECTRON MICROSCOPY (3.4 Å)