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A histone octamer-like structure within TFIID

A histone octamer-like structure within TFIID THE general transcription factor TFIID nucleates initiation complex formation through direct core promoter binding1,2, commits promoters within chromatin to transcription3, and mediates the action of transcriptional activators, a phenomenon that may correlate with enhanced TFIID recruitment4–7 or conformational changes in TFIID-promoter complexes8,9. Molecular studies of the multiprotein TFIID complex have identified a primary TATA binding subunit (TBP)2, TBP-associated factors (TAFs) that interact with and mediate the function of activators2,7,10,11 and intersubunit interactions2 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 homo-logies in the human TFIID subunits hTAFSO, hTAF31 and hTAF20/15. Together with analyses of native TFIID complexes and accompanying crystallographic studies12, the results suggest that there is a histone octamer-like TAF complex within TFIID. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Nature Springer Journals

A histone octamer-like structure within TFIID

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References (28)

Publisher
Springer Journals
Copyright
Copyright © 1996 by Nature Publishing Group
Subject
Science, Humanities and Social Sciences, multidisciplinary; Science, Humanities and Social Sciences, multidisciplinary; Science, multidisciplinary
ISSN
0028-0836
eISSN
1476-4687
DOI
10.1038/380356a0
Publisher site
See Article on Publisher Site

Abstract

THE general transcription factor TFIID nucleates initiation complex formation through direct core promoter binding1,2, commits promoters within chromatin to transcription3, and mediates the action of transcriptional activators, a phenomenon that may correlate with enhanced TFIID recruitment4–7 or conformational changes in TFIID-promoter complexes8,9. Molecular studies of the multiprotein TFIID complex have identified a primary TATA binding subunit (TBP)2, TBP-associated factors (TAFs) that interact with and mediate the function of activators2,7,10,11 and intersubunit interactions2 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 homo-logies in the human TFIID subunits hTAFSO, hTAF31 and hTAF20/15. Together with analyses of native TFIID complexes and accompanying crystallographic studies12, the results suggest that there is a histone octamer-like TAF complex within TFIID.

Journal

Nature – Springer Journals

Published: Mar 28, 1996

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