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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HIV-1 Tat protein increases transcriptional initiation and stabilizes elongation
Laspia, M. F., Rice, A. P., & Mathews, M. B. (1989) · Cell · doi:10.1016/0092-8674(89)90290-0 · Cited by 571
Purification of P-TEFb, a Transcription Factor Required for the Transition into Productive Elongation
Marshall, N. F., & Price, D. H. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.21.12335 · Cited by 564
Self-citation
The MO15 cell cycle kinase is associated with the TFIIH transcription-DNA repair factor
Roy, R., Adamczewski, J. P., Seroz, T., Vermeulen, W., Tassan, J., Schaeffer, L., Nigg, E. A., Hoeijmakers, J. H. J., & Egly, J. (1994) · Cell · doi:10.1016/0092-8674(94)90039-6 · Cited by 439
Cdk-activating kinase complex is a component of human transcription factor TFIIH
Shiekhattar, R., Mermelstein, F. H., Fisher, R. P., Drapkin, R., Dynlacht, B. D., Wessling, H. C., Morgan, D. O., & Reinberg, D. (1995) · Nature · doi:10.1038/374283a0 · Cited by 431
Relationship of CDK-activating kinase and RNA polymerase II CTD kinase TFIIH/TFIIK
Feaver, W. J., Svejstrup, J. Q., Henry, N. L., & Kornberg, R. D. (1994) · Cell · doi:10.1016/0092-8674(94)90040-x · Cited by 427
A kinase–cyclin pair in the RNA polymerase II holoenzyme
Liao, S.-M., Zhang, J., Jeffery, D., Koleske, A. J., Thompson, C. M., Chao, D. M., Viljoen‐Bloom, M., Vuuren, H. J. J. V., & Young, R. A. (1995) · Nature · doi:10.1038/374193a0 · Cited by 419
Human general transcription factor IIH phosphorylates the C-terminal domain of RNA polymerase II
Lu, H., Zawel, L. S., Fisher, L., Egly, J., & Reinberg, D. (1992) · Nature · doi:10.1038/358641a0 · Cited by 402
Ku autoantigen is the regulatory component of a template-associated protein kinase that phosphorylates RNA polymerase II.
Dvir, A., Peterson, S., Knuth, M. W., Lu, H., & Dynan, W. S. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.24.11920 · Cited by 371
Association of Cdk-activating kinase subunits with transcription factor TFIIH
Serizawa, H., Mäkelä, T. P., Conaway, J. W., Conaway, R. C., Weinberg, R. A., & Young, R. A. (1995) · Nature · doi:10.1038/374280a0 · Cited by 367

Flagged first, then by citations

Show all 69 references

Research works printed but not linked: 14

Spencer, 1990, Oncogene, 5, 777
Meulia, 1993, Mol. Cell. Biol., 13, 5647
Collart, 1991, Mol. Cell. Biol., 11, 2826
Yue, 1993, Mol. Cell. Biol., 13, 3191
Ramamurthy, 1990, Mol. Cell. Biol., 10, 1484
Middleton, 1990, Mol. Cell Biol., 10, 727
Hair, 1993, Mol. Cell. Biol., 13, 7925
Krauskopf, 1991, Mol. Cell. Biol., 11, 3515
Rougvie, 1990, Mol. Cell. Biol., 10, 6041
Kephart, 1992, Mol. Cell. Biol., 12, 2067
Marshall, 1992, Mol. Cell. Biol., 12, 2078
Bartolomei, 1988, Mol. Cell. Biol., 8, 330
Allison, 1988, Mol. Cell. Biol., 8, 321
Lee, 1992, Gene Exp., 1, 149

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Kim, J. B., Yamaguchi, Y., Wada, T., Handa, H., & Sharp, P. A. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.9.5960 · Cited by 53
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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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