ArticleeLife2021
Cryo-EM structure of the yeast TREX complex and coordination with the SR-like protein Gbp2.
Article in eLife, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 43 citations in OpenAlex.
- Conserved mRNP remodeling mechanism of the TREX-2.1 complex.Nucleic acids research · 2026Article
- Bridging technical innovation and computational advances in studies of RNA-protein assemblies.Nature reviews. Genetics · 2026Review
- Molecular insights into mRNA export regulation by the human TREX-2 complex.Nature communications · 2026Article
- Structure, function and assembly of nuclear pore complexes.Nature reviews. Molecular cell biology · 2026Review
- Article
- Unraveling gene expression: a beginner's guide from chromatin modifications to mRNA export inNucleus (Austin, Tex.) · 2025Review
- From transcription to export: mRNA's winding path to the cytoplasm.Trends in biochemical sciences · 2025Review
- A time-resolved framework for the recruitment of mRNP processing and assembly factors to a site of transcription.Nucleic acids research · 2025Article
- Structural mechanism of DDX39B regulation by human TREX-2 and a related complex in mRNP remodeling.Nature communications · 2025Article
- Structures and mRNP remodeling mechanism of the TREX-2 complex.Structure (London, England : 1993) · 2025Article
- Cryo-EM structure of the CBC-ALYREF complex.eLife · 2024Article
- Critical Cellular Functions and Mechanisms of Action of the RNA Helicase UAP56.Journal of molecular biology · 2024Review
- Article
- mRNA nuclear export: how mRNA identity features distinguish functional RNAs from junk transcripts.RNA biology · 2024Review
- Tho2 is critical for the recruitment of Rrp6 to chromatin in response to perturbed mRNP biogenesis.RNA (New York, N.Y.) · 2023Article
- Cross-linking mass spectrometric analysis of the endogenous TREX complex fromRNA (New York, N.Y.) · 2023Article
- Single-molecule quantitation of RNA-binding protein occupancy and stoichiometry defines a role for Yra1 (Aly/REF) in nuclear mRNP organization.Cell reports · 2023Article
- New advances in cross-linking mass spectrometry toward structural systems biology.Current opinion in chemical biology · 2023Review
- Cellular functions of eukaryotic RNA helicases and their links to human diseases.Nature reviews. Molecular cell biology · 2023Review
- Structural basis for high-order complex of SARNP and DDX39B to facilitate mRNP assembly.Cell reports · 2023Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.