Document Detail


The architecture of human general transcription factor TFIID core complex.
MedLine Citation:
PMID:  23292512     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
The initiation of gene transcription by RNA polymerase II is regulated by a plethora of proteins in human cells. The first general transcription factor to bind gene promoters is transcription factor IID (TFIID). TFIID triggers pre-initiation complex formation, functions as a coactivator by interacting with transcriptional activators and reads epigenetic marks. TFIID is a megadalton-sized multiprotein complex composed of TATA-box-binding protein (TBP) and 13 TBP-associated factors (TAFs). Despite its crucial role, the detailed architecture and assembly mechanism of TFIID remain elusive. Histone fold domains are prevalent in TAFs, and histone-like tetramer and octamer structures have been proposed in TFIID. A functional core-TFIID subcomplex was revealed in Drosophila nuclei, consisting of a subset of TAFs (TAF4, TAF5, TAF6, TAF9 and TAF12). These core subunits are thought to be present in two copies in holo-TFIID, in contrast to TBP and other TAFs that are present in a single copy, conveying a transition from symmetry to asymmetry in the TFIID assembly pathway. Here we present the structure of human core-TFIID determined by cryo-electron microscopy at 11.6 Å resolution. Our structure reveals a two-fold symmetric, interlaced architecture, with pronounced protrusions, that accommodates all conserved structural features of the TAFs including the histone folds. We further demonstrate that binding of one TAF8-TAF10 complex breaks the original symmetry of core-TFIID. We propose that the resulting asymmetric structure serves as a functional scaffold to nucleate holo-TFIID assembly, by accreting one copy each of the remaining TAFs and TBP.
Authors:
Christoph Bieniossek; Gabor Papai; Christiane Schaffitzel; Frederic Garzoni; Maxime Chaillet; Elisabeth Scheer; Petros Papadopoulos; Laszlo Tora; Patrick Schultz; Imre Berger
Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2013-1-06
Journal Detail:
Title:  Nature     Volume:  -     ISSN:  1476-4687     ISO Abbreviation:  Nature     Publication Date:  2013 Jan 
Date Detail:
Created Date:  2013-1-7     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0410462     Medline TA:  Nature     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Affiliation:
1] European Molecular Biology Laboratory (EMBL) Grenoble Outstation, and Unit of Virus Host Cell Interactions UVHCI, UJF-CNRS-EMBL Unité Mixte International UMI 3265, 6 rue Jules Horowitz, 38042 Grenoble Cedex 9, France [2].
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