TI  - Molecular cloning and expression of the 32-kDa subunit of human   <prot>TFIID</prot>  
      reveals interactions with  <prot>VP16</prot>  and  <prot>TFIIB</prot>  that mediate transcriptional
      activation.
PG  - 5788-92
AB  - Transcription factor <prot>TFIID</prot> consists of <prot>TATA binding protein</prot> (<prot>TBP</prot>) and at
      least eight <prot>TBP</prot>-associated factors (TAF). As TAFs are required for
      activated but not basal transcription, we have proposed that <prot>TAF</prot>s act as
      coactivators to mediate signals between activators and the basal
      transcription machinery. Here we report the cloning, expression, and
      biochemical characterization of the 32-kDa subunit of human (h) <prot>TFIID</prot>,
      termed <prot>hTAFII32</prot>. We find that <prot>hTAFII32</prot> is the human homologue of
      Drosophila <prot>TAFII40</prot>. In vitro protein-protein interaction assays reveal
      that as observed with Drosophila <prot>TAFII40</prot>,   <prot>hTAFII32</prot>   interacts with the
      C-terminal 39-amino acid activation domain of the acidic transactivator
       <prot>viral protein 16</prot> (<prot>VP16</prot>)  as well as with the general transcription factor
       <prot>TFIIB</prot> . Moreover, a partial recombinant <prot>TFIID</prot> complex containing <prot>hTAFII32</prot>
      was capable of mediating in vitro transcriptional activation by the <prot>VP16</prot>
      activation domain. These findings indicate that specific
      activator-coactivator interactions have been conserved between human and
      Drosophila and provide additional support for the function of these
      interactions in mediating transcriptional activation.
AD  - Howard Hughes Medical Institute, Department of Molecular and Cell Biology,
