ArticleNature communications2017
The conserved protein Seb1 drives transcription termination by binding RNA polymerase II and nascent RNA.
Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed.
- Transcriptional PBR cycles at pericentromeric repeats cause gross chromosomal rearrangements through Rad52-dependent ADR-loop formation.Nucleic acids research · 2026Article
- Conserved protein Seb1 that interacts with RNA polymerase II and RNA is an antipausing transcription elongation factor.RNA (New York, N.Y.) · 2025Article
- Overexpression of the RNA-binding protein NrdA affects global gene expression and secondary metabolism inmSphere · 2025Article
- DSIF factor Spt5 coordinates transcription, maturation and exoribonucleolysis of RNA polymerase II transcripts.Nature communications · 2025Article
- Multiple Forms and Functions of Premature Termination by RNA Polymerase II.Journal of molecular biology · 2025Review
- DEAD-box ATPase Dbp2 is the key enzyme in an mRNP assembly checkpoint at the 3'-end of genes and involved in the recycling of cleavage factors.Nature communications · 2024Article
- Repression of pervasive antisense transcription is the primary role of fission yeast RNA polymerase II CTD serine 2 phosphorylation.Nucleic acids research · 2024Article
- Polyadenylated versions of small non-coding RNAs inMicrobial cell (Graz, Austria) · 2024Article
- Experimental phasing opportunities for macromolecular crystallography at very long wavelengths.Communications chemistry · 2023Article
- Advantages and limitations of UV cross-linking analysis of protein-RNA interactomes in microbes.Molecular microbiology · 2023Review
- The conserved RNA-binding protein Seb1 promotes cotranscriptional ribosomal RNA processing by controlling RNA polymerase I progression.Nature communications · 2023Article
- Isha is a su(Hw) mRNA-binding protein required for gypsy insulator function.G3 (Bethesda, Md.) · 2022Article
- Transcription and chromatin-based surveillance mechanism controls suppression of cryptic antisense transcription.Cell reports · 2021Article
- Genetic screen for suppression of transcriptional interference identifies a gain-of-function mutation in Pol2 termination factor Seb1.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- What's all the phos about? Insights into the phosphorylation state of the RNA polymerase II C-terminal domainRSC chemical biology · 2021Review
- System-wide analyses of the fission yeast poly(A)Genome research · 2020Article
- Nutrient-dependent control of RNA polymerase II elongation rate regulates specific gene expression programs by alternative polyadenylation.Genes & development · 2020Article
- Termination of non-coding transcription in yeast relies on both an RNA Pol II CTD interaction domain and a CTD-mimicking region in Sen1.The EMBO journal · 2020Article
- RNA Exosomes and Their Cofactors.Methods in molecular biology (Clifton, N.J.) · 2020Review
- Autonomous Pathway:Plant physiology · 2020Article
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13 authors.
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Abstract
Termination of RNA polymerase II (Pol II) transcription is an important step in the transcription cycle, which involves the dislodgement of polymerase from DNA, leading to release of a functional transcript. Recent studies have identified the key players required for this process and showed that a common feature of these proteins is a conserved domain that interacts with the phosphorylated C-terminus of Pol II (CTD-interacting domain, CID). However, the mechanism by which transcription termination is achieved is not understood. Using genome-wide methods, here we show that the fission yeast CID-protein Seb1 is essential for termination of protein-coding and non-coding genes through interaction with S2-phosphorylated Pol II and nascent RNA. Furthermore, we present the crystal structures of the Seb1 CTD- and RNA-binding modules. Unexpectedly, the latter reveals an intertwined two-domain arrangement of a canonical RRM and second domain. These results provide important insights into the mechanism underlying eukaryotic transcription termination.
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