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PMID: 2725511 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Dynamic interaction between a Drosophila transcription factor and RNA polymerase II.

Molecular and cellular biology ·Vol. 9 ·No. 4 ·1989-04-00 ·Pages 1465-75

Price DH, Sluder AE, Greenleaf AL

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.

MeSH Terms
Animals Drosophila/genetics,metabolism Kinetics Protein Conformation RNA Polymerase II/metabolism Transcription Factors/isolation & purification,metabolism Transcription, Genetic
Chemicals
Transcription Factors RNA Polymerase II
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Price D H
Department of Biochemistry, Duke University Medical Center, Durham, North Carolina 27710.
Sluder A E
Greenleaf A L
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Article Info
Journal
Molecular and cellular biology
Abbr.
Mol Cell Biol
ISSN
0270-7306
DOI
10.1128/mcb.9.4.1465-1475.1989
Published
1989-04-00
Pages
1465-75
Language
English
Region
United States
NLM ID
8109087
PMCID
PMC362563
Subset
IM
Grants
NIGMS NIH HHS · GM28078 · United States
NIGMS NIH HHS · GM35500 · United States
External Links
PubMed source DOI: 10.1128/mcb.9.4.1465-1475.1989 PMC Full Text View journal details
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