Cited by 666Genomics and Chromatin DynamicsRNA Research and SplicingNuclear Structure and Function

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Control of RNA Polymerase II Elongation Potential by a Novel Carboxyl-terminal Domain Kinase

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Marshall, Nick F., Peng, Junmin, Xie, Zhi, Price, David H.·1996·Journal of Biological Chemistry

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Abstract

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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Authors: Marshall, N. F., Peng, J., Xie, Z., & Price, D. H.
Affiliations: University of Iowa (US)
Corresponding author: Price, David H.
ORCID: Peng, Junmin
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)
DOI: 10.1074/jbc.271.43.27176
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: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 8801 d)
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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Control of RNA Polymerase II Elongation Potential by a Novel Carboxyl-terminal Domain Kinase

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