7LUV

Cryo-EM structure of the yeast THO-Sub2 complex

Summary for 7LUV

• Entry DOI: 10.2210/pdb7luv/pdb
• EMDB information: 23527
• Descriptor: THO complex subunit HPR1, THO complex subunit THP2, THO complex subunit 2, ... (6 entities in total)
• Functional Keywords: nuclear mrna export, dead-box atpase, mrnp remodeling, rna binding protein
• Biological source: Saccharomyces cerevisiae (Baker's yeast); More
• Total number of polymer chains: 6
• Total formula weight: 361439.92

Authors

Xie, Y.,Ren, Y. (deposition date: 2021-02-23, release date: 2021-04-14, Last modification date: 2024-03-06)

Primary citation

Xie, Y.,Clarke, B.P.,Kim, Y.J.,Ivey, A.L.,Hill, P.S.,Shi, Y.,Ren, Y.
Cryo-EM structure of the yeast TREX complex and coordination with the SR-like protein Gbp2.
Elife, 10:-, 2021

PubMed Abstract: The evolutionarily conserved TRanscript-EXport (TREX) complex plays central roles during mRNP (messenger ribonucleoprotein) maturation and export from the nucleus to the cytoplasm. In yeast, TREX is composed of the THO sub-complex (Tho2, Hpr1, Tex1, Mft1, and Thp2), the DEAD box ATPase Sub2, and Yra1. Here we present a 3.7 Å cryo-EM structure of the yeast THO•Sub2 complex. The structure reveals the intimate assembly of THO revolving around its largest subunit Tho2. THO stabilizes a semi-open conformation of the Sub2 ATPase via interactions with Tho2. We show that THO interacts with the serine-arginine (SR)-like protein Gbp2 through both the RS domain and RRM domains of Gbp2. Cross-linking mass spectrometry analysis supports the extensive interactions between THO and Gbp2, further revealing that RRM domains of Gbp2 are in close proximity to the C-terminal domain of Tho2. We propose that THO serves as a landing pad to configure Gbp2 to facilitate its loading onto mRNP.

PubMed: 33787496
DOI: 10.7554/eLife.65699

Experimental method

ELECTRON MICROSCOPY (3.7 Å)