Dynamic interaction between a Drosophila transcription factor and RNA polymerase II.
Open Access
- 1 April 1989
- journal article
- research article
- Published by Taylor & Francis in Molecular and Cellular Biology
- Vol. 9 (4) , 1465-1475
- https://doi.org/10.1128/mcb.9.4.1465
Abstract
We have purified factor 5, a Drosophila RNA polymerase II transcription factor. Factor 5 was found to be required for accurate initiation of transcription from specific promoters and also had a dramatic effect on the elongation properties of RNA polymerase II. Kinetic studies suggested that factor 5 stimulates the elongation rate of RNA polymerase II on a dC-tailed, double-stranded template by reducing the time spent at the numerous pause sites encountered by the polymerase. The factor was found to be composed of two polypeptides (34 and 86 kilodaltons). Both subunits bound tightly to pure RNA polymerase II but were not bound to polymerase in elongation complexes. Our results suggest that factor 5 interacts briefly with the paused polymerase molecules and catalyzes a conformational change in them such that they adopt an elongation-competent conformation.This publication has 46 references indexed in Scilit:
- Renaturase and ribonuclease H: a novel mechanism that influences transcript displacement by RNA polymerase II in vitroBiochemistry, 1988
- An elongation control particle containing the N gene transcriptional antitermination protein of bacteriophage lambdaCell, 1987
- A general transcription factor forms a stable complex with RNA polymerase B (II)Published by Elsevier ,1987
- Identification of intrinsic termination sites in vitro for RNA polymerase II within eukaryotic gene sequencesJournal of Molecular Biology, 1987
- Mapping and characterization of transcriptional pause sites in the early genetic region of bacteriophage T7Journal of Molecular Biology, 1987
- Transcriptional selectivity of viral genes in mammalian cellsCell, 1986
- Interaction of a gene-specific transcription factor with the adenovirus major late promoter upstream of the TATA box regionCell, 1985
- Interaction of the sigma factor and the nusA gene protein of E. coli with RNA polymerase in the initiation-termination cycle of transcriptionCell, 1981
- Purification of a factor from Ehrlich ascites tumor cells specifically stimulating RNA polymerase IIBiochemistry, 1976
- Stimulation of in vitro transcription by ribonuclease H (hybridase)FEBS Letters, 1972