ArticleNucleic acids research1997
Heat-shock inactivation of the TFIIH-associated kinase and change in the phosphorylation sites on the C-terminal domain of RNA polymerase II.
Article in Nucleic acids research, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 58 citations in OpenAlex.
- RNA polymerase II transcription initiation in holo-TFIID-depleted mouse embryonic stem cells.Cell reports · 2024Article
- An Important Role for RPRD1B in the Heat Shock Response.Molecular and cellular biology · 2022Article
- The pause-initiation limit restricts transcription activation in human cells.Nature communications · 2019Article
- Interplay between RNA interference and heat shock response systems in Drosophila melanogaster.Open biology · 2016Article
- TFIIH subunit alterations causing xeroderma pigmentosum and trichothiodystrophy specifically disturb several steps during transcription.American journal of human genetics · 2015Article
- Stress induces changes in the phosphorylation of Trypanosoma cruzi RNA polymerase II, affecting its association with chromatin and RNA processing.Eukaryotic cell · 2014Article
- The C-terminal domain of RNA polymerase II functions as a phosphorylation-dependent splicing activator in a heterologous protein.Molecular and cellular biology · 2005Article
- Multisite phosphorylation of Pin1-associated mitotic phosphoproteins revealed by monoclonal antibodies MPM-2 and CC-3.BMC cell biology · 2004Article
- RNA polymerase II carboxy-terminal domain kinases: emerging clues to their function.Eukaryotic cell · 2002Review
- Stress-specific activation and repression of heat shock factors 1 and 2.Molecular and cellular biology · 2001Article
- Article
- The binding of the alpha subunit of protein kinase CK2 and RAP74 subunit of TFIIF to protein-coding genes in living cells is DRB sensitive.Molecular and cellular biochemistry · 1999Article
- Heat shock factor increases the reinitiation rate from potentiated chromatin templates.Molecular and cellular biology · 1998Article
- Nuclear translocation and carboxyl-terminal domain phosphorylation of RNA polymerase II delineate the two phases of zygotic gene activation in mammalian embryos.The EMBO journal · 1997Article
- Components of the human SWI/SNF complex are enriched in active chromatin and are associated with the nuclear matrix.The Journal of cell biology · 1997Article
- Article
- A uniform procedure for the purification of CDK7/CycH/MAT1, CDK8/CycC and CDK9/CycT1.Biological procedures onlineArticle
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The C-terminal domain (CTD) of the RNA polymerase II largest subunit (RPB1) plays a central role in transcription. The CTD is unphosphorylated when the polymerase assembles into a preinitiation complex of transcription and becomes heavily phosphorylated during promoter clearance and entry into elongation of transcription. A kinase associated to the general transcription factor TFIIH, in the preinitiation complex, phosphorylates the CTD. The TFIIH-associated CTD kinase activity was found to decrease in extracts from heat-shocked HeLa cells compared to unstressed cells. This loss of activity correlated with a decreased solubility of the TFIIH factor. The TFIIH-kinase impairment during heat-shock was accompanied by the disappearance of a particular phosphoepitope (CC-3) on the RPB1 subunit. The CC-3 epitope was localized on the C-terminal end of the CTD and generated in vitro when the RPB1 subunit was phosphorylated by the TFIIH-associated kinase but not by another CTD kinase such as MAP kinase. In apparent discrepancy, the overall RPB1 subunit phosphorylation increased during heat-shock. The decreased activity in vivo of the TFIIH kinase might be compensated by a stress-activated CTD kinase such as MAP kinase. These results also suggest that heat-shock gene transcription may have a weak requirement for TFIIH kinase activity.
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