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Structure. 2009 Nov 11;17(11):1442-52. doi: 10.1016/j.str.2009.09.007.

Cryo-EM reveals promoter DNA binding and conformational flexibility of the general transcription factor TFIID.

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1
Department of Structural Biology, Fairchild Building, Stanford University School of Medicine, Stanford, CA 94305, USA. hael@stanford.edu

Abstract

The general transcription factor IID (TFIID) is required for initiation of RNA polymerase II-dependent transcription at many eukaryotic promoters. TFIID comprises the TATA-binding protein (TBP) and several conserved TBP-associated factors (TAFs). Recognition of the core promoter by TFIID assists assembly of the preinitiation complex. Using cryo-electron microscopy in combination with methods for ab initio single-particle reconstruction and heterogeneity analysis, we have produced density maps of two conformational states of Schizosaccharomyces pombe TFIID, containing and lacking TBP. We report that TBP-binding is coupled to a massive histone-fold domain rearrangement. Moreover, docking of the TBP-TAF1(N-terminus) atomic structure to the TFIID map and reconstruction of a TAF-promoter DNA complex helps to account for TAF-dependent regulation of promoter-TBP and promoter-TAF interactions.

PMID:
19913479
DOI:
10.1016/j.str.2009.09.007
[Indexed for MEDLINE]
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