+Search query
-Structure paper
Title | Structure of the human core transcription-export complex reveals a hub for multivalent interactions. |
---|---|
Journal, issue, pages | Elife, Vol. 9, Year 2020 |
Publish date | Nov 16, 2020 |
Authors | Thomas Pühringer / Ulrich Hohmann / Laura Fin / Belén Pacheco-Fiallos / Ulla Schellhaas / Julius Brennecke / Clemens Plaschka / |
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 ...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. |
External links | Elife / PubMed:33191911 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.3 - 4.7 Å |
Structure data | EMDB-11853: EMDB-11854: EMDB-11855: EMDB-11856: EMDB-11857: Structure of the human THO - UAP56 complex (Map B) |
Source |
|
Keywords | GENE REGULATION / mRNA / nucleocytoplasmic transport / R-loop / gene expression |