Control of RNA polymerase II elongation potential by a novel carboxyl-terminal domain kinase.
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.
Mesh Terms:
Hydrolysis, Phosphorylation, Protein Kinases, RNA Polymerase II, Transcription Factor TFIIH, Transcription Factors, Transcription Factors, TFII
Hydrolysis, Phosphorylation, Protein Kinases, RNA Polymerase II, Transcription Factor TFIIH, Transcription Factors, Transcription Factors, TFII
J. Biol. Chem.
Date: Oct. 25, 1996
PubMed ID: 8900211
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