Abstract：
:The general transcription factor TFIID is a multiprotein complex containing the TATA-binding protein and several associated factors (TAFs), some of which may function as coactivators that are essential for activated, but not basal, transcription. Here we describe the isolation and characterization of the first gene encoding a TAF protein. The deduced amino acid sequence of TAF110 revealed the presence of several glutamine- and serine/threonine-rich regions reminiscent of the protein-protein interaction domains of the regulatory transcription factor Sp1 that are involved in transcription activation and multimerization. In both Drosophila cells and yeast, TAF110 specifically interacts with the glutamine-rich activation domains of Sp1. Moreover, purified Sp1 selectively binds recombinant TAF110 in vitro. These findings taken together suggest that TAF110 may function as a coactivator by serving as a site of protein-protein contact between activators like Sp1 and the TFIID complex.
journal_name
Celljournal_title
Cellauthors
Hoey T,Weinzierl RO,Gill G,Chen JL,Dynlacht BD,Tjian Rdoi
10.1016/0092-8674(93)90664-csubject
Has Abstractpub_date
1993-01-29 00:00:00pages
247-60issue
2eissn
0092-8674issn
1097-4172pii
0092-8674(93)90664-Cjournal_volume
72pub_type
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