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A Histone Octamer-Like Structure Within TFIID

A Histone Octamer-Like Structure Within TFIID

A Hoffmann, C M Chiang, T Oelgeschläger, X Xie, S K Burley, Y Nakatani, R G Roeder

Nature. 1996 Mar 28;380(6572):356-9.

PMID: 8598932

Abstract:

The general transcription factor TFIID 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 TFIID recruitment or conformational changes in TFIID-promoter complexes. Molecular studies of the multiprotein TFIID complex have identified a primary TATA binding subunit (TBP), 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 TFIID subunits hTAF80, hTAF31 and hTAF20/15. Together with analyses of native TFIID complexes and accompanying crystallographic studies, the results suggest that there is a histone octamer-like TAF complex within TFIID.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
IAR42414923	TFIID, native complex human			Price

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