7APK

Structure of the human THO - UAP56 complex

7APK の概要

• エントリーDOI: 10.2210/pdb7apk/pdb
• EMDBエントリー: 11853 11854 11855 11856 11857
• 分子名称: THO complex subunit 1, THO complex subunit 2, THO complex subunit 3, ... (8 entities in total)
• 機能のキーワード: mrna, nucleocytoplasmic transport, r-loop, gene expression, gene regulation
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 30
• 化学式量合計: 1836843.28

構造登録者

Hohmann, U.,Puehringer, T.,Plaschka, C. (登録日: 2020-10-17, 公開日: 2020-12-16, 最終更新日: 2024-05-01)

主引用文献

Puhringer, T.,Hohmann, U.,Fin, L.,Pacheco-Fiallos, B.,Schellhaas, U.,Brennecke, J.,Plaschka, C.
Structure of the human core transcription-export complex reveals a hub for multivalent interactions.
Elife, 9:-, 2020

PubMed Abstract: The export of mRNA from nucleus to cytoplasm requires the conserved and essential transcription and export (TREX) complex (THO-UAP56/DDX39B-ALYREF). TREX selectively binds mRNA maturation marks and licenses mRNA for nuclear export by loading the export factor NXF1-NXT1. How TREX integrates these marks and achieves high selectivity for mature mRNA is poorly understood. Here, we report the cryo-electron microscopy structure of the human THO-UAP56/DDX39B complex at 3.3 Å resolution. The seven-subunit THO-UAP56/DDX39B complex multimerizes into a 28-subunit tetrameric assembly, suggesting that selective recognition of mature mRNA is facilitated by the simultaneous sensing of multiple, spatially distant mRNA regions and maturation marks. Two UAP56/DDX39B RNA helicases are juxtaposed at each end of the tetramer, which would allow one bivalent ALYREF protein to bridge adjacent helicases and regulate the TREX-mRNA interaction. Our structural and biochemical results suggest a conserved model for TREX complex function that depends on multivalent interactions between proteins and mRNA.

PubMed: 33191911
DOI: 10.7554/eLife.61503

実験手法

ELECTRON MICROSCOPY (3.3 Å)