TI  - Cloning of an intrinsic human <prot>TFIID</prot> subunit that interacts with multiple
      transcriptional activators.
PG  - 531-6
AB  - <prot>TFIID</prot> is a multisubunit protein complex comprised of the  <prot>TATA-binding
      protein</prot> (<prot>TBP</prot>)  and multiple  TBP-associated factors (TAFs) . The TAFs in
      <prot>TFIID</prot> are essential for activator-dependent transcription. The cloning of
      a complementary DNA encoding a human <prot>TFIID</prot> TAF, <prot>TAFII55</prot>, that has no known
      homolog in Drosophila <prot>TFIID</prot> is now described.      <prot>TAFII55</prot>      is shown to interact
      with the largest subunit ( <prot>TAFII230</prot> ) of human <prot>TFIID</prot> through its central
      region and with multiple activators--including  <prot>Sp1</prot> ,  <prot>YY1</prot> ,  <prot>USF</prot> ,  <prot>CTF</prot> ,
      adenoviral <prot>E1A</prot>, and human immunodeficiency virus-type 1 <prot>Tat</prot>
      proteins--through a distinct amino-terminal domain. The
       <prot>TAFII55</prot> -interacting region of  <prot>Sp1</prot>  was localized to its DNA-binding domain,
      which is distinct from the glutamine-rich activation domains previously
      shown to interact with Drosophila <prot>TAFII110</prot>. Thus, this human <prot>TFIID</prot> TAF may
      be a co-activator that mediates a response to multiple activators through
      a distinct mechanism.
AD  - Laboratory of Biochemistry and Molecular Biology, Rockefeller University,
