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Control of RNA Polymerase II Elongation Potential by a Novel Carboxyl-terminal Domain Kinase
Open accessAbstract
The entry of RNA polymerase II into a productive mode of elongation is controlled, in part, by the postinitiation activity of positive transcription elongation factor b (P-TEFb) (Marshall, N. F., and Price, D. H. (1995) J. Biol. Chem. 270, 12335-12338). We report here that removal of the carboxyl-terminal domain (CTD) of the large subunit of RNA polymerase II abolishes productive elongation. Correspondingly, we found that P-TEFb can phosphorylate the CTD of pure RNA polymerase II. Furthermore, P-TEFb can phosphorylate the CTD of RNA polymerase II when the polymerase is in an early elongation complex. Both the function and kinase activity of P-TEFb are blocked by the drugs 5, 6-dichloro-1-beta-D-ribofuranosylbenzimidazole (DRB) and H-8. P-TEFb is distinct from transcription factor IIH (TFIIH) because the two factors have no subunits in common, P-TEFb is more sensitive to DRB than is TFIIH, and most importantly, TFIIH cannot substitute functionally for P-TEFb. We propose that phosphorylation of the CTD by P-TEFb controls the transition from abortive into productive elongation mode.
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“Phosphorylation of Ser5 of the Pol II CTD by transcription factor IIH (TFIIH) is required for transcription initiation, whereas phosphorylation of Ser2 of the Pol II CTD, of DSIF (DRB sensitivity inducing factor) and of NELF (negative elongation factor) by pTEFb (positive transcription elongation factor) is needed for transcription elongation141–143.”
From Molecular regulation of stem cell quiescence (2013) · cites this paper as [143]
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Metadata
- Authors
- Marshall, N. F., Peng, J., Xie, Z., & Price, D. H.
- Affiliations
- University of Iowa (US)
- Corresponding author
- Price, David H.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1996-10
- Volume
- 271
- Issue
- 43
- Pages
- 27176-27183
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2020329201
- Cited by
- 662
- References
- 69
- Citations by year
- 2026: 11 · 2025: 7 · 2024: 16 · 2023: 20 · 2022: 11 · 2021: 15 · 2020: 20 · 2019: 19 · 2018: 13 · 2017: 13 · 2016: 18 · 2015: 27 · 2014: 20 · 2013: 30 · 2012: 27
- FWCI
- 11.86
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- Yale University
- National Institute of General Medical Sciences (R01GM035500, GM-35500)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- Keywords
- RNA polymerase II, transcription elongation, C-terminal domain, P-TEFb, CTD phosphorylation, DRB, H-8, TFIIH, kinase activity
- MeSH terms
- Hydrolysis, Phosphorylation, Protein Kinases, RNA Polymerase II, Transcription Factors, Transcription Factors, TFII, Transcription Factor TFIIH
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