ArticleThe Journal of biological chemistry2011
The functions of TFIIF during initiation and transcript elongation are differentially affected by phosphorylation by casein kinase 2.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 20 citations in OpenAlex.
- Protein kinase CK2 - diverse roles in cancer cell biology and therapeutic promise.Molecular and cellular biochemistry · 2023Review
- Review
- Dynamics of the RNA polymerase I TFIIF/TFIIE-like subcomplex: a mini-review.Biochemical Society transactions · 2020Review
- Gdown1 Associates Efficiently with RNA Polymerase II after Promoter Clearance and Displaces TFIIF during Transcript Elongation.PloS one · 2016Article
- Ccr4-Not and TFIIS Function Cooperatively To Rescue Arrested RNA Polymerase II.Molecular and cellular biology · 2015Article
- Transcription factors TFIIF and TFIIS promote transcript elongation by RNA polymerase II by synergistic and independent mechanisms.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Functional interactions of the RNA polymerase II-interacting proteins Gdown1 and TFIIF.The Journal of biological chemistry · 2014Article
- The RNA polymerase II preinitiation complex. Through what pathway is the complex assembled?Transcription · 2014Review
- RNA polymerase II transcription elongation control.Chemical reviews · 2013Review
- Single-molecule studies of RNAPII elongation.Biochimica et biophysica acta · 2013Review
- Inactivated RNA polymerase II open complexes can be reactivated with TFIIE.The Journal of biological chemistry · 2012Article
- Transcription factor TFIIF is not required for initiation by RNA polymerase II, but it is essential to stabilize transcription factor TFIIB in early elongation complexes.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Defining the divergent enzymatic properties of RNA polymerases I and II.The Journal of biological chemistryArticle
- Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The RNA polymerase II (pol II) initiation and elongation factor elongation factor TFIIF can be extensively phosphorylated in vivo, although the significance of this modification has not been clear. We now show that phosphorylation of recombinant TFIIF by casein kinase 2 (CK2) reduces or eliminates some of the functions of TFIIF while paradoxically leaving others intact. Phospho-IIF is fully functional in binding to free pol II and is able to support the initiation of transcription. However, the phosphorylated factor does not bind to stalled elongation complexes as measured in a gel mobility shift assay. Significantly, phosphorylation strongly reduces (or for some truncated versions of RAP74, eliminates) stimulation of transcript elongation by TFIIF. Thus, although TFIIF must participate at the initiation of transcription, its ability to continue its association with pol II and stimulate transcript elongation can be specifically regulated by CK2. This is particularly interesting because CK2 is required for initiation at a subset of pol II promoters. Modulation of TFIIF function could be important in controlling promoter-proximal pausing by pol II during the early stage of transcript elongation.
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Registered trials
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