TI  - A histone octamer-like structure within <prot>TFIID</prot>.
PG  - 356-9
AB  - The general transcription factor <prot>TFIID</prot> nucleates initiation complex
      formation through direct core promoter binding, commits promoters within
      chromatin to transcription, and mediates the action of transcriptional
      activators, a phenomenon that may correlate with enhanced <prot>TFIID</prot>
      recruitment or conformational changes in <prot>TFIID</prot>-promoter complexes.
      Molecular studies of the multiprotein <prot>TFIID</prot> complex have identified a
      primary  <prot>TATA binding subunit</prot> (<prot>TBP</prot>) ,  TBP-associated factors (TAFs)  that
      interact with and mediate the function of activators and intersubunit
      interactions but have yielded relatively little insight into the
      structural organization of the complex or the actual mechanism of
      transcriptional activation. Here we present biochemical evidence for the
      structural relevance of histone homologies in the human <prot>TFIID</prot> subunits
       <prot>hTAF80</prot> ,  <prot>hTAF31</prot>  and  <prot>hTAF20/15</prot> . Together with analyses of native <prot>TFIID</prot>
      complexes and accompanying crystallographic studies, the results suggest
      that there is a histone octamer-like TAF complex within <prot>TFIID</prot>.
AD  - Laboratory of Biochemistry and Molecular Biology, The Rockefeller
