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ISOLATION OF COACTIVATORS ASSOCIATED WITH THE TATA-BINDING PROTEIN THAT MEDIATE TRANSCRIPTIONAL ACTIVATION
Author(s): DYNLACHT BD, HOEY T, TJIAN R
Source: CELL    Volume: 66    Issue: 3    Pages: 563-576    Published: AUG 9 1991  
Times Cited: 543     References: 40     
Abstract: A key step in the regulation of transcription involves interactions between promoter-selective factors and various components of the transcriptional apparatus. Here we report the requirements for transcriptional activation directed by NTF-1, a developmentally regulated transcription factor in Drosophila. Reconstituted transcription with fractionated Drosophila basal factors reveals that activation by NTF-1 requires factors present in the endogenous TFIID fraction that are distinct from the purified TATA-binding protein (TBP). Glycerol gradient sedimentation and immunoprecipitation analyses indicate that TFIID is a multiprotein complex containing TBP and at least six tightly bound TBP-associated factors (TAFs). Preparations of TBP lacking TAFs after fractionation with denaturants no longer support activation by NTF-1 but retain basal level activity. Addition of immunopurified and renatured TAFs to free TBP restores the ability of NTF-1 to activate transcription without influencing basal transcription. These results suggest that one or more of the TAF polypeptides confer coactivator function.
Document Type: Article
Language: English
Reprint Address: DYNLACHT, BD (reprint author), UNIV CALIF BERKELEY, HOWARD HUGHES MED INST, DEPT MOLEC & CELL BIOL, BERKELEY, CA 94720 USA
Publisher: CELL PRESS, 1050 MASSACHUSETTES AVE, CIRCULATION DEPT, CAMBRIDGE, MA 02138
Subject Category: Biochemistry & Molecular Biology; Cell Biology
IDS Number: GA941
ISSN: 0092-8674
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