TFIID is a multiprotein complex with a molecular mass of around 750 kDa that directs pre-initiation complex assembly on both TATA box-containing and TATA-less promoters. It consists of TATA-binding protein (TBP) and a number of TBP associated factors (TAFs). TBP alone can replace TFIID in a reconstituted in vitro transcription system but only the TFIID complex can mediate transcriptional activation. TAFII250, the largest subunit of TFIID contains protein kinase and histone acetyltransferase activities linking transcriptional initiation/activation with chromatin modification. In addition, multiple serine/ threonine phosphorylations of TBP and TAFs selectively inhibit the ability of TFIID to mediate transcriptional activation.
Physical form
Clear and colorless frozen liquid solution
Preparation Note
Use a manual defrost freezer and avoid repeated freeze-thaw cycles. While working, please keep sample on ice.
The Journal of biological chemistry, 255(24), 11992-11996 (1980-12-25)
A soluble extract prepared from human cells (KB S-100) has been recently shown to direct accurate transcription initiation by purified RNA polymerase II at the major late promoter of adenovirus 2. We have fractionated this extract by chromatography on phosphocellulose
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
Some TAF subunits of transcription factor TFIID play a pivotal role in transcriptional activation by mediating protein-protein interactions, whereas other TAFs direct promoter selectivity via protein-DNA recognition. Here, we report that purified recombinant TAFII250 is a protein serine kinase that
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