Control of formation of two distinct classes of RNA polymerase II elongation complexes.
Open Access
- 1 May 1992
- journal article
- Published by Taylor & Francis in Molecular and Cellular Biology
- Vol. 12 (5), 2078-2090
- https://doi.org/10.1128/mcb.12.5.2078
Abstract
We have examined elongation by RNA polymerase II initiated at a promoter and have identified two classes of elongation complexes. Following initiation at a promoter, all polymerase molecules enter an abortive mode of elongation. Abortive elongation is characterized by the rapid generation of short transcripts due to pausing of the polymerase followed by termination of transcription. Termination of the early elongation complexes can be suppressed by the addition of 250 mM KCl or 1 mg of heparin per ml soon after initiation. Elongation complexes of the second class carry out productive elongation in which long transcripts can be synthesized. Productive elongation complexes are derived from early paused elongation complexes by the action of a factor which we call P-TEF (positive transcription elongation factor). P-TEF is inhibited by 5,6-dichloro-1-beta-D-ribofuranosylbenzimidazole at concentrations which have no effect on the initiation of transcription. By using templates immobilized on paramagnetic particles, we show that isolated preinitiation complexes lack P-TEF and give rise to transcription complexes which can carry out only abortive elongation. The ability to carry out productive elongation can be restored to isolated transcription complexes by the addition of P-TEF after initiation. A model is presented which describes the role of elongation factors in the formation and maintenance of elongation complexes. The model is consistent with the available in vivo data concerning control of elongation and is used to predict the outcome of other potential in vitro and in vivo experiments.Keywords
This publication has 85 references indexed in Scilit:
- CTD kinase associated with yeast RNA polymerase II initiation factor bCell, 1991
- Identification and purification of a yeast protein that affects elongation by RNA polymerase IIJournal of Biological Chemistry, 1991
- Promoter-dependent phosphorylation of RNA polymerase II by a template-bound kinase. Association with transcriptional initiationJournal of Biological Chemistry, 1991
- Blocking of Tat-dependent HIV-1 RNA modification by an inhibitor of RNA polymerase II processivityNature, 1991
- Role of the mammalian transcription factors IIF, IIS, and IIX during elongation by RNA polymerase II.Molecular and Cellular Biology, 1991
- Requirement for the .beta.,.gamma.-pyrophosphate bond of ATP in a stage between transcription initiation and elongation by Escherichia coli RNA polymeraseBiochemistry, 1991
- Modulation of a constitutive transcriptional block at exon-1 controls human c-myc oncogene expression.1990
- Assembly and disassembly of the Drosophila RNA polymerase II complex during transcription.Journal of Biological Chemistry, 1990
- The block to transcription elongation at the SV40 attenuation site is decreased in vitro by oligomers complementary to segments of the attenuator RNAGene, 1989
- HIV-1 Tat protein increases transcriptional initiation and stabilizes elongationCell, 1989