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PMID: 8464492 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Largest subunit of Drosophila transcription factor IID directs assembly of a complex containing TBP and a coactivator.

Nature ·Vol. 362 ·No. 6420 ·1993-04-08 ·Pages 511-7

Weinzierl RO, Dynlacht BD, Tjian R

Abstract

The TFIID complex consists of the TATA-binding protein (TBP) and associated factors (TAFs) serving to mediate transcriptional activation by promoter-specific regulators. Here we report the cloning of Drosophila TAFII250 and the assembly of a partial complex containing recombinant TBP, TAFII110 and the C-terminal domain of TAFII250. This triple complex supports Sp1 activation and reveals specific interactions between TAFII250, TBP and TAFII110.

MeSH Terms
Amino Acid Sequence Animals Cloning, Molecular DNA-Binding Proteins/genetics,physiology Drosophila/genetics Histone Acetyltransferases Molecular Sequence Data Nuclear Proteins/genetics Recombinant Proteins Sp1 Transcription Factor/physiology TATA-Binding Protein Associated Factors TATA-Box Binding Protein Transcription Factor TFIID Transcription Factors/physiology Transcriptional Activation
Chemicals
DNA-Binding Proteins Nuclear Proteins Recombinant Proteins Sp1 Transcription Factor TATA-Binding Protein Associated Factors TATA-Box Binding Protein Transcription Factor TFIID Transcription Factors Histone Acetyltransferases TATA-binding protein associated factor 250 kDa
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Weinzierl R O
Howard Hughes Medical Institute, Department of Molecular and Cell Biology, University of California, Berkeley 94720.
Dynlacht B D
Tjian R
Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
DOI
10.1038/362511a0
Published
1993-04-08
Pages
511-7
Language
English
Region
England
NLM ID
0410462
Subset
IM
External Links
PubMed source DOI: 10.1038/362511a0 View journal details
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