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(Received for publication, June 5, 1996, and in revised form, July 19, 1996)
From the Department of Biochemistry, University of Iowa,
Iowa City, Iowa 52242
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-
Volume 271, Number 43,
Issue of October 25, 1996
pp. 27176-27183
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
-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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