A histone octamer-like structure within TFIID

Alexander Hoffmann, Cheng Ming Chiang, Thomas Oelgeschläger, Xiaoling Xie, Stephen K. Burley, Yoshihiro Nakatani, Robert G. Roeder

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154 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)356-359
Number of pages4
JournalNature
Volume380
Issue number6572
DOIs
StatePublished - Mar 28 1996

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    Hoffmann, A., Chiang, C. M., Oelgeschläger, T., Xie, X., Burley, S. K., Nakatani, Y., & Roeder, R. G. (1996). A histone octamer-like structure within TFIID. Nature, 380(6572), 356-359. https://doi.org/10.1038/380356a0