ArticleNature structural & molecular biology2012
Structural basis for the assembly and nucleic acid binding of the TREX-2 transcription-export complex.
Article in Nature structural & molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.
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Who cites it
76 citing papers in PubMed, 122 citations in OpenAlex.
- Conserved mRNP remodeling mechanism of the TREX-2.1 complex.Nucleic acids research · 2026Article
- Sus1 Modulates Chromatin Remodeling and Gene Expression via the Cell Wall Integrity Pathway in Saccharomyces cerevisiae.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026Article
- TREX2 component PCID2 scaffolds alternative SAC3-based subcomplexes with distinct RNA processing and export function.bioRxiv : the preprint server for biology · 2026Article
- Acetic acid induces proteasome storage granule formation and inhibits proteasomal proteolysis: Comparison with other induction conditions.The Journal of biological chemistry · 2026Article
- Molecular insights into mRNA export regulation by the human TREX-2 complex.Nature communications · 2026Article
- The Arabidopsis Mutant of the Small Intrinsically Disordered Protein DSS1(V) Exhibits Increased Sensitivity to Drought Stress.Plant direct · 2026Article
- Article
- Unraveling gene expression: a beginner's guide from chromatin modifications to mRNA export inNucleus (Austin, Tex.) · 2025Review
- Nup153 and TPR/Megator Interact with TREX-2 Subunits and Are Essential for TREX-2-Dependent Nuclear Export ofInternational journal of molecular sciences · 2025Article
- Identification of divergentbioRxiv : the preprint server for biology · 2025Article
- Interdomain Interactions of the PCID2 Protein, One of the Subunits of the TREX-2 mRNA Export Complex in Drosophila melanogaster.Doklady. Biochemistry and biophysics · 2025Article
- Two RNA-Binding Regions of PCID2, a Subunit of the TREX-2 mRNA Nuclear Export Complex, Competitively Interact with the 3' Noncoding Region of ras2 mRNA.Doklady. Biochemistry and biophysics · 2025Article
- DSS1 is required for proper Integrator-PP2A function.Nature communications · 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
- Detailed characterisation of the trypanosome nuclear pore architecture reveals conserved asymmetrical functional hubs that drive mRNA export.PLoS biology · 2025Article
- A natural PCID2-Targeting compound suppresses hepatocellular carcinoma progression: evidence from structure-based discovery and biological evaluation.Frontiers in pharmacology · 2025Article
- Xmas-2 Protein, the Core Protein of the TREX-2 mRNA Export Complex, Does not Determine the Specificity of ras2 mRNA Binding by the Complex.Doklady. Biochemistry and biophysics · 2024Article
- Point Mutations in the M Domain of PCID2 Impair Its Function in mRNA Export in Drosophila melanogaster.Doklady biological sciences : proceedings of the Academy of Sciences of the USSR, Biological sciences sections · 2024Article
- Assessing Transcriptomic Responses to Oxidative Stress: Contrasting Wild-Type Arabidopsis Seedlings withInternational journal of molecular sciences · 2024Article
16 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
The conserved TREX-2 transcription-export complex integrates transcription and processing of many actively transcribed nascent mRNAs with the recruitment of export factors at nuclear pores and also contributes to transcriptional memory and genomic stability. We report the crystal structure of the Sac3-Thp1-Sem1 segment of Saccharomyces cerevisiae TREX-2 that interfaces with the gene expression machinery. Sac3-Thp1-Sem1 forms a previously uncharacterized PCI-domain complex characterized by the juxtaposition of Sac3 and Thp1 winged helix domains, forming a platform that mediates nucleic acid binding. Our structure-guided mutations support the idea that the Thp1-Sac3 interaction is an essential requirement for mRNA binding and for the coupling of transcription and processing to mRNP assembly and export. These results provide insight into how newly synthesized transcripts are efficiently transferred from TREX-2 to the principal mRNA export factor, and they reveal how Sem1 stabilizes PCI domain-containing proteins and promotes complex assembly.
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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.