ArticleMolecular and cellular biology2011
New suppressors of THO mutations identify Thp3 (Ypr045c)-Csn12 as a protein complex involved in transcription elongation.
Article in Molecular and cellular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed, 16 citations in OpenAlex.
- Conserved mRNP remodeling mechanism of the TREX-2.1 complex.Nucleic acids research · 2026Article
- TREX2 component PCID2 scaffolds alternative SAC3-based subcomplexes with distinct RNA processing and export function.bioRxiv : the preprint server for biology · 2026Article
- Structural assembly of the nucleic-acid-binding Thp3-Csn12-Sem1 complex functioning in mRNA splicing.Nucleic acids research · 2022Article
- Promoter-Terminator Gene Loops Affect Alternative 3'-End Processing in Yeast.The Journal of biological chemistry · 2016Article
- Nuclear pore components affect distinct stages of intron-containing gene expression.Nucleic acids research · 2015Article
- A novel factor Iss10 regulates Mmi1-mediated selective elimination of meiotic transcripts.Nucleic acids research · 2013Article
- Structural basis for the assembly and nucleic acid binding of the TREX-2 transcription-export complex.Nature structural & molecular biology · 2012Article
- Transcriptional elongation and mRNA export are coregulated processes.Genetics research international · 2011Article
- Structural biology of the PCI-protein fold.BioarchitectureReview
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7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Formation of a ribonucleoprotein particle (mRNP) competent for export requires the coupling of transcription with mRNA processing and RNA export. A key link between these processes is provided by the THO complex. To progress in our understanding of this coupling, we have performed a search for suppressors of the transcription defect caused by the hpr1Δ mutation. This has permitted us to identify mutations in the genes for the RNA polymerase II mediator component Med10, the Sch9 protein kinase, and the Ypr045c protein. We report a role in transcription elongation for Ypr045c (Thp3) and the Csn12 component of the COP9 signalosome. Thp3 and Csn12 form a complex that is recruited to transcribed genes. Their mutations suppress the gene expression defects of THO complex mutants involved in mRNP biogenesis and export and show defects in mRNA accumulation. Transcription elongation impairment of thp3Δ mutants is shown by in vivo transcript run-on analysis performed in G-less systems. Thp3-Csn12 establishes a novel link between transcription and mRNA processing that opens new perspectives on our understanding of gene expression and reveals novel functions for a component of the COP9 signalosome. Thp3-Csn12 also copurifies with ribosomal proteins, which opens the possibility that it has other functions in addition to transcription.
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