4TRQ

Crystal structure of Sac3/Thp1/Sem1

Summary for 4TRQ

• Entry DOI: 10.2210/pdb4trq/pdb
• Descriptor: Nuclear mRNA export protein SAC3, Nuclear mRNA export protein THP1, 26S proteasome complex subunit SEM1, ... (4 entities in total)
• Functional Keywords: pci domain, trex-2, gene expression, gene regulation
• Biological source: Saccharomyces cerevisiae (Baker's yeast); More
• Cellular location: Nucleus envelope : P46674 Q08231
• Total number of polymer chains: 6
• Total formula weight: 151771.85

Authors

Hellerschmied, D.,Schneider, S.,Kohler, A.,Clausen, T. (deposition date: 2014-06-17, release date: 2015-08-26, Last modification date: 2023-12-20)

Primary citation

Schneider, M.,Hellerschmied, D.,Schubert, T.,Amlacher, S.,Vinayachandran, V.,Reja, R.,Pugh, B.F.,Clausen, T.,Kohler, A.
The Nuclear Pore-Associated TREX-2 Complex Employs Mediator to Regulate Gene Expression.
Cell, 162:1016-1028, 2015

PubMed Abstract: Nuclear pore complexes (NPCs) influence gene expression besides their established function in nuclear transport. The TREX-2 complex localizes to the NPC basket and affects gene-NPC interactions, transcription, and mRNA export. How TREX-2 regulates the gene expression machinery is unknown. Here, we show that TREX-2 interacts with the Mediator complex, an essential regulator of RNA Polymerase (Pol) II. Structural and biochemical studies identify a conserved region on TREX-2, which directly binds the Mediator Med31/Med7N submodule. TREX-2 regulates assembly of Mediator with the Cdk8 kinase and is required for recruitment and site-specific phosphorylation of Pol II. Transcriptome and phenotypic profiling confirm that TREX-2 and Med31 are functionally interdependent at specific genes. TREX-2 additionally uses its Mediator-interacting surface to regulate mRNA export suggesting a mechanism for coupling transcription initiation and early steps of mRNA processing. Our data provide mechanistic insight into how an NPC-associated adaptor complex accesses the core transcription machinery.

PubMed: 26317468
DOI: 10.1016/j.cell.2015.07.059

Experimental method

X-RAY DIFFRACTION (3.1 Å)