ArticleProceedings of the National Academy of Sciences of the United States of America1997
A role for TFIIH in controlling the activity of early RNA polymerase II elongation complexes.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
55 citing papers in PubMed, 127 citations in OpenAlex.
- Transcription start site scanning requires the fungi-specific hydrophobic loop of Tfb3.Nucleic acids research · 2024Article
- Structural visualization of de novo transcription initiation by Saccharomyces cerevisiae RNA polymerase II.Molecular cell · 2022Article
- Filgotinib suppresses HIV-1-driven gene transcription by inhibiting HIV-1 splicing and T cell activation.The Journal of clinical investigation · 2020Article
- The capping enzyme facilitates promoter escape and assembly of a follow-on preinitiation complex for reinitiation.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Insight into promoter clearance by RNA polymerase II.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- TFIIE orchestrates the recruitment of the TFIIH kinase module at promoter before release during transcription.Nature communications · 2019Article
- Transcription factors that influence RNA polymerases I and II: To what extent is mechanism of action conserved?Biochimica et biophysica acta. Gene regulatory mechanisms · 2017Review
- Specific Inhibition of HIV Infection by the Action of Spironolactone in T Cells.Journal of virology · 2016Article
- Function of Conserved Topological Regions within the Saccharomyces cerevisiae Basal Transcription Factor TFIIH.Molecular and cellular biology · 2016Article
- Transcription Start Site Scanning and the Requirement for ATP during Transcription Initiation by RNA Polymerase II.The Journal of biological chemistry · 2016Article
- Structure of an RNA polymerase II preinitiation complex.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Plasmodium falciparum XPD translocates in 5' to 3' direction, is expressed throughout the blood stages, and interacts with p44.Protoplasma · 2015Article
- Article
- Uncoupling Promoter Opening from Start-Site Scanning.Molecular cell · 2015Article
- Double-stranded DNA translocase activity of transcription factor TFIIH and the mechanism of RNA polymerase II open complex formation.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- TFIIH subunit alterations causing xeroderma pigmentosum and trichothiodystrophy specifically disturb several steps during transcription.American journal of human genetics · 2015Article
- In TFIIH, XPD helicase is exclusively devoted to DNA repair.PLoS biology · 2014Article
- Promoter clearance by RNA polymerase II.Biochimica et biophysica acta · 2013Review
- TFIIH: when transcription met DNA repair.Nature reviews. Molecular cell biology · 2012Review
- Enzymatic activities and DNA substrate specificity of Mycobacterium tuberculosis DNA helicase XPB.PloS one · 2012Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
TFIIH is a multifunctional RNA polymerase II transcription factor that possesses DNA-dependent ATPase, DNA helicase, and protein kinase activities. Previous studies have established that TFIIH enters the preinitiation complex and fulfills a critical role in initiation by catalyzing ATP-dependent formation of the open complex prior to synthesis of the first phosphodiester bond of nascent transcripts. In this report, we present direct evidence that TFIIH also controls RNA polymerase II activity at a postinitiation stage of transcription, by preventing premature arrest by very early elongation complexes just prior to their transition to stably elongating complexes. Unexpectedly, we observe that TFIIH is capable of entering the transcription cycle not only during assembly of the preinitiation complex but also after initiation and synthesis of as many as four to six phosphodiester bonds. These findings shed new light on the role of TFIIH in initiation and promoter escape and reveal an unanticipated flexibility in the ability of TFIIH to interact with RNA polymerase II transcription intermediates prior to, during, and immediately after initiation.
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Registered trials
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.