ArticleProceedings of the National Academy of Sciences of the United States of America2007
The transcription elongation factor TFIIS is a component of RNA polymerase II preinitiation complexes.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.
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Who cites it
75 citing papers in PubMed, 106 citations in OpenAlex.
- Muscleblind-like proteins dimerize by forming disulfide bonds to regulate alternative splicing and pathogenic RNA foci formation.Nucleic acids research · 2026Article
- pka1 deletion induces hyperactivation of the transcription factor Mca1 and drives chromosome mis-segregation in Schizosaccharomyces pombe.Molecular genetics and genomics : MGG · 2026Article
- Muscleblind-like proteins dimerize by forming disulfide bonds to regulate alternative splicing and pathogenic RNA foci formation.bioRxiv : the preprint server for biology · 2026Article
- Transcriptional PBR cycles at pericentromeric repeats cause gross chromosomal rearrangements through Rad52-dependent ADR-loop formation.Nucleic acids research · 2026Article
- A lethal ORC ATPase mutation is suppressed by alterations in ORC and RNA Pol II transcription components.PloS one · 2026Article
- Domain acquisition enabled functional expansion of the TFIIS transcription factor family.Cell & bioscience · 2025Review
- Differential impact of divalent metals on native elongating transcript sequencing (NET-seq) protocols for RNA polymerases I and II.PloS one · 2025Article
- Article
- The general transcription factors (GTFs) of RNA polymerase II and their roles in plant development and stress responses.Critical reviews in biochemistry and molecular biology · 2024Review
- Structural basis for evolutionarily conserved interactions between TFIIS and Paf1C.International journal of biological macromolecules · 2023Article
- Involvement of the MGF 110-11L Gene in the African Swine Fever Replication and Virulence.Vaccines · 2023Article
- The TFIIS N-terminal domain (TND): a transcription assembly module at the interface of order and disorder.Biochemical Society transactions · 2023Review
- Structural basis of a transcription pre-initiation complex on a divergent promoter.Molecular cell · 2023Article
- Elongation factor TFIIS is essential for heat stress adaptation in plants.Nucleic acids research · 2022Article
- Multi-Omics Approach Reveals miR-SNPs Affecting Muscle Fatty Acids Profile in Nelore Cattle.Genes · 2021Article
- The African Swine Fever Virus Transcriptome.Journal of virology · 2020Article
- Structure and mechanism of the RNA polymerase II transcription machinery.Genes & development · 2020Review
- Elongation Factor TFIIS Prevents Transcription Stress and R-Loop Accumulation to Maintain Genome Stability.Molecular cell · 2019Article
- A Novel Assay for RNA Polymerase I Transcription Elongation Sheds Light on the Evolutionary Divergence of Eukaryotic RNA Polymerases.Biochemistry · 2019Article
- Cold Acclimation Improves the Desiccation Stress Resilience of Polar Strains ofFrontiers in microbiology · 2019Article
15 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
In this article, we provide direct evidence that the evolutionarily conserved transcription elongation factor TFIIS functions during preinitiation complex assembly. First, we identified TFIIS in a mass spectrometric screen of RNA polymerase II (Pol II) preinitiation complexes (PICs). Second, we show that the association of TFIIS with a promoter depends on functional PIC components including Mediator and the SAGA complex. Third, we demonstrate that TFIIS is required for efficient formation of active PICs. Using truncation mutants of TFIIS, we find that the Pol II-binding domain is the minimal domain necessary to stimulate PIC assembly. However, efficient formation of active PICs requires both the Pol II-binding domain and the poorly understood N-terminal domain. Importantly, Domain III, which is required for the elongation function of TFIIS, is dispensable during PIC assembly. The results demonstrate that TFIIS is a PIC component that is required for efficient formation and/or stability of the complex.
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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.