ArticleThe EMBO journal2012
Architecture and nucleic acids recognition mechanism of the THO complex, an mRNP assembly factor.
Article in The EMBO journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.
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Who cites it
54 citing papers in PubMed.
- Unraveling gene expression: a beginner's guide from chromatin modifications to mRNA export inNucleus (Austin, Tex.) · 2025Review
- Cellular imbalance of specific RNA-binding proteins associates with harmful R-loops.PLoS genetics · 2025Article
- Intrinsically disordered RNA-binding motifs cooperate to catalyze RNA folding and drive phase separation.Nucleic acids research · 2024Article
- TREX tetramer disruption alters RNA processing necessary for corticogenesis in THOC6 Intellectual Disability Syndrome.Nature communications · 2024Article
- Compromised transcription-mRNA export factor THOC2 causes R-loop accumulation, DNA damage and adverse neurodevelopment.Nature communications · 2024Article
- 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
- Structural basis for high-order complex of SARNP and DDX39B to facilitate mRNP assembly.Cell reports · 2023Article
- Nuclear mRNPs are compact particles packaged with a network of proteins promoting RNA-RNA interactions.Genes & development · 2023Article
- THOC5 complexes with DDX5, DDX17, and CDK12 to regulate R loop structures and transcription elongation rate.iScience · 2023Article
- The RNA export and RNA decay complexes THO and TRAMP prevent transcription-replication conflicts, DNA breaks, and CAG repeat contractions.PLoS biology · 2022Article
- Maturation and shuttling of the yeast telomerase RNP: assembling something new using recycled parts.Current genetics · 2022Review
- Harmful R-loops are prevented via different cell cycle-specific mechanisms.Nature communications · 2021Article
- Cryo-EM structure of the yeast TREX complex and coordination with the SR-like protein Gbp2.eLife · 2021Article
- Article
- Structural insights into the nucleic acid remodeling mechanisms of the yeast THO-Sub2 complex.eLife · 2020Article
- Structure of the human core transcription-export complex reveals a hub for multivalent interactions.eLife · 2020Article
- ARTP/EMS-combined multiple mutagenesis efficiently improved production of raw starch-degrading enzymes in Penicillium oxalicum and characterization of the enzyme-hyperproducing mutant.Biotechnology for biofuels · 2020Article
- UAP56/DDX39B is a major cotranscriptional RNA-DNA helicase that unwinds harmful R loops genome-wide.Genes & development · 2020Article
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13 authors.
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No grant is acknowledged in the PubMed record.
Abstract
The THO complex is a key factor in co-transcriptional formation of export-competent messenger ribonucleoprotein particles, yet its structure and mechanism of chromatin recruitment remain unknown. In yeast, this complex has been described as a heterotetramer (Tho2, Hpr1, Mft1, and Thp2) that interacts with Tex1 and mRNA export factors Sub2 and Yra1 to form the TRanscription EXport (TREX) complex. In this study, we purified yeast THO and found Tex1 to be part of its core. We determined the three-dimensional structures of five-subunit THO complex by electron microscopy and located the positions of Tex1, Hpr1, and Tho2 C-terminus using various labelling techniques. In the case of Tex1, a β-propeller protein, we have generated an atomic model which docks into the corresponding part of the THO complex envelope. Furthermore, we show that THO directly interacts with nucleic acids through the unfolded C-terminal region of Tho2, whose removal reduces THO recruitment to active chromatin leading to mRNA biogenesis defects. In summary, this study describes the THO architecture, the structural basis for its chromatin targeting, and highlights the importance of unfolded regions of eukaryotic proteins.
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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.