Isolation of coactivators associated with the TATA-binding protein that mediate transcriptional activation.

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.

journal_name

Cell

journal_title

Cell

authors

Dynlacht BD,Hoey T,Tjian R

doi

10.1016/0092-8674(81)90019-2

subject

Has Abstract

pub_date

1991-08-09 00:00:00

pages

563-76

issue

3

eissn

0092-8674

issn

1097-4172

pii

0092-8674(81)90019-2

journal_volume

66

pub_type

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