Journal article
Purification of an RNA polymerase II transcript release factor from Drosophila
The Journal of biological chemistry, Vol.271(19), pp.11043-11046
05/10/1996
DOI: 10.1074/jbc.271.19.11043
PMID: 8626643
Abstract
Factor 2 was previously identified in Drosophila Kc cell nuclear extract (KcN) as an activity suppressing the appearance of long transcripts (Price, D. H., Sluder, A. E., and Greenleaf, A. L. (1987) J. Biol. Chem. 262, 3244-3255). A 154-kDa protein with factor 2 activity was purified to apparent homogeneity from KcN. An immobilized template assay indicated that factor 2 caused the release of transcripts by RNA polymerase II in an ATP-dependent manner. Some early elongation complexes were resistant to factor 2 action but became sensitive after treatment with 1 M KCl. In the absence of factor 2, transcription complexes still exhibited a low degree of processivity suggesting that factor 2 was only partially responsible for abortive elongation.
Details
- Title: Subtitle
- Purification of an RNA polymerase II transcript release factor from Drosophila
- Creators
- Zhi Xie - Department of Biochemistry, University of Iowa, Iowa City 52242, USADavid H Price
- Resource Type
- Journal article
- Publication Details
- The Journal of biological chemistry, Vol.271(19), pp.11043-11046
- DOI
- 10.1074/jbc.271.19.11043
- PMID
- 8626643
- NLM abbreviation
- J Biol Chem
- ISSN
- 0021-9258
- eISSN
- 1083-351X
- Publisher
- United States
- Grant note
- R01-GM35500 / NIGMS NIH HHS
- Language
- English
- Date published
- 05/10/1996
- Academic Unit
- Biochemistry and Molecular Biology
- Record Identifier
- 9984024503502771
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