A complex of two TFIID TATA box-binding protein-associated factors (TAF(II)s) is described at 2.0 Å resolution. The amino-terminal portions of dTAF(II)42 and dTAF(II)62 from Drosophila adopt the canonical histone fold, consisting of two short α-helices flanking a long central α-helix. Like histones H3 and H4, dTAF(II)42 and dTAF(II)62 form an intimate heterodimer by extensive hydrophobic contacts between the paired molecules. In solution and in the crystalline state, the dTAF(II)42/dTAF(II)62 complex exists as a heterotetramer, resembling the (H3/H4), heterotetrameric core of the histone octamer, suggesting that TFIID contains a histone octamer-like substructure.
|Original language||English (US)|
|Number of pages||7|
|State||Published - Mar 28 1996|
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