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TAF7 is a heat-inducible unstable protein and is required for sustained expression of heat shock protein genes.
- Source :
-
The FEBS journal [FEBS J] 2018 Sep; Vol. 285 (17), pp. 3215-3224. Date of Electronic Publication: 2018 Aug 18. - Publication Year :
- 2018
-
Abstract
- TATA-binding protein-associated factor 7 (TAF7), a dissociable component of the general transcription factor IID (TFIID), plays a role as a check-point regulator at the step of RNA polymerase II (Pol II) transcription initiation. Here, we focused on the role of TAF7 in heat-shocked cells, where its expression is induced by heat shock factor HSF1. TAF7 is a phosphoprotein, and the phosphorylation status is related to its interaction with TFIID and to its stability controlled by the ubiquitin-proteasome pathway. TAF7 is necessary for the prolonged expression of heat shock protein genes and for efficient recovery of heat-shocked cells. During sustained transcription, TAF7, presumably its TFIID-independent form, binds the promoter and enhances the levels of Pol II at the gene body but not the promoter. These results showed the novel function of TAF7 that is necessary for the transition from initiation to elongation in multiple-round transcription.<br /> (© 2018 Federation of European Biochemical Societies.)
- Subjects :
- HeLa Cells
Heat Shock Transcription Factors genetics
Heat Shock Transcription Factors metabolism
Heat-Shock Proteins genetics
Humans
Phosphorylation
Protein Stability
Proteolysis
TATA-Binding Protein Associated Factors chemistry
TATA-Binding Protein Associated Factors genetics
Transcription Factor TFIID chemistry
Transcription Factor TFIID genetics
Transcription Initiation Site
Transcription, Genetic
Ubiquitin metabolism
Gene Expression Regulation
Heat-Shock Proteins metabolism
Heat-Shock Response
Promoter Regions, Genetic
TATA-Binding Protein Associated Factors metabolism
Transcription Factor TFIID metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1742-4658
- Volume :
- 285
- Issue :
- 17
- Database :
- MEDLINE
- Journal :
- The FEBS journal
- Publication Type :
- Academic Journal
- Accession number :
- 30028080
- Full Text :
- https://doi.org/10.1111/febs.14604