EMD-5134
TBP-containing S. pombe TFIID
EMD-5134
Single-particle8.0 Å
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Map released: 02/11/2009
Last modified: 10/01/2011
Sample: Native S. pombe TFIID
Deposition Authors: Elmlund H
,
Baraznenok V,
Linder T
,
Szilagyi Z,
Rofougaran R,
Hofer A
,
Hebert H,
Lindahl M,
Gustafsson CM
Deposition Authors: Elmlund H
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Cryo-EM reveals promoter DNA binding and conformational flexibility of the general transcription factor TFIID.
Elmlund H
,
Baraznenok V,
Linder T
,
Szilagyi Z,
Rofougaran R,
Hofer A
,
Hebert H,
Lindahl M,
Gustafsson CM
(2009) Structure , 17 , 1442 - 1452
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(2009) Structure , 17 , 1442 - 1452
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.
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.