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Structural similarity between TAFs and the heterotetrameric core of the histone octamer

Abstract

A complex of two TFIID TATA box-binding protein-associated factors (TAFIIs) is described at 2.0 Å resolution. The amino-terminal portions of dTAFII42 and dTAFII62 from Drosophila adopt the canonical histone fold, consisting of two short α-helices flanking a long central α-helix. Like histones H3 and H4, dTAFII42 and dTAFII62 form an intimate heterodimer by extensive hydrophobic contacts between the paired molecules. In solution and in the crystalline state, the dTAFII42/dTAFII62 complex exists as a heterotetramer, resembling the (H3/H4)2 heterotetrameric core of the histone octamer, suggesting that TFIID contains a histone octamer-like substructure.

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