7AQO

yeast THO-Sub2 complex dimer

7AQO の概要

• エントリーDOI: 10.2210/pdb7aqo/pdb
• EMDBエントリー: 11871
• 分子名称: THO complex subunit 2, THO complex subunit HPR1, TEX1 isoform 1, ... (6 entities in total)
• 機能のキーワード: yeast tho complex s. cerevisiae tho-sub2 the transcription-export (trex) complex, rna binding protein
• 由来する生物種: Saccharomyces cerevisiae S288C; 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 864451.02

構造登録者

Schuller, S.K.,Schuller, J.M.,Prabu, R.J.,Baumgartner, M.,Bonneau, F.,basquin, J.,Conti, E. (登録日: 2020-10-22, 公開日: 2020-12-02, 最終更新日: 2024-05-01)

主引用文献

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

実験手法

ELECTRON MICROSCOPY (4.5 Å)