Journal article
Control of RNA Polymerase II Elongation Potential by a Novel Carboxyl-terminal Domain Kinase
The Journal of biological chemistry, Vol.271(43), pp.27176-27183
10/25/1996
DOI: 10.1074/jbc.271.43.27176
PMID: 8900211
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.
Details
- Title: Subtitle
- Control of RNA Polymerase II Elongation Potential by a Novel Carboxyl-terminal Domain Kinase
- Creators
- Nick F MarshallJunmin PengZhi XieDavid H Price
- Resource Type
- Journal article
- Publication Details
- The Journal of biological chemistry, Vol.271(43), pp.27176-27183
- DOI
- 10.1074/jbc.271.43.27176
- PMID
- 8900211
- NLM abbreviation
- J Biol Chem
- ISSN
- 0021-9258
- eISSN
- 1083-351X
- Language
- English
- Date published
- 10/25/1996
- Academic Unit
- Biochemistry and Molecular Biology
- Record Identifier
- 9984025272702771
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