ArticleNucleic acids research2017
Structure of the Sac3 RNA-binding M-region in the Saccharomyces cerevisiae TREX-2 complex.
Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 14 citations in OpenAlex.
- 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
- Molecular insights into mRNA export regulation by the human TREX-2 complex.Nature communications · 2026Article
- Article
- Peculiarities of theInternational journal of molecular sciences · 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
- 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
- A Protein-Protein Interaction Analysis Suggests a Wide Range of New Functions for the p21-Activated Kinase (PAK) Ste20.International journal of molecular sciences · 2023Article
- Structural assembly of the nucleic-acid-binding Thp3-Csn12-Sem1 complex functioning in mRNA splicing.Nucleic acids research · 2022Article
- Telomeric C-circles localize at nuclear pore complexes in Saccharomyces cerevisiae.The EMBO journal · 2022Article
- Evolution and diversification of the nuclear pore complex.Biochemical Society transactions · 2021Review
- Distinct effects on mRNA export factor GANP underlie neurological disease phenotypes and alter gene expression depending on intron content.Human molecular genetics · 2020Article
- Mechanisms of nuclear mRNA export: A structural perspective.Traffic (Copenhagen, Denmark) · 2019Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Transcription-export complex 2 (TREX-2, or THSC) facilitates localization of actively transcribing genes such as GAL1 to the nuclear periphery, contributes to the generation of export-competent mRNPs and influences gene expression through interactions with Mediator. TREX-2 is based on a Sac3 scaffold to which Thp1, Sem1, Cdc31 and Sus1 bind and consists of three modules: the N-region (Sac3∼1-100), which binds mRNA export factor Mex67:Mtr2; the M-region, in which Thp1 and Sem1 bind to Sac3∼100-550; and the CID region in which Cdc31 and two Sus1 chains bind to Sac3∼720-805. Although the M-region of Sac3 was originally thought to encompass residues ∼250-550, we report here the 2.3Å resolution crystal structure of a complex containing Sac3 residues 60-550 that indicates that the TPR-like repeats of the M-region extend to residue 137 and that residues 90-125 form a novel loop that links Sac3 to Thp1. These new structural elements are important for growth and mRNA export in vivo. Although deleting Sac3 residues 1-90 produced a wild-type phenotype, deletion of the loop as well generated growth defects at 37°C, whereas the deletion of residues 1-250 impaired mRNA export and also generated longer lag times when glucose or raffinose was replaced by galactose as the carbon source.
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