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TitleThe architecture of human general transcription factor TFIID core complex.
Journal, issue, pagesNature, Vol. 493, Issue 7434, Page 699-702, Year 2013
Publish dateJan 31, 2013
AuthorsChristoph Bieniossek / Gabor Papai / Christiane Schaffitzel / Frederic Garzoni / Maxime Chaillet / Elisabeth Scheer / Petros Papadopoulos / Laszlo Tora / Patrick Schultz / Imre Berger /
PubMed AbstractThe 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 ...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.
External linksNature / PubMed:23292512
MethodsEM (single particle)
Resolution11.6 - 14.3 Å
Structure data

EMDB-2229:
The architecture of human general transcription factor TFIID core complex
Method: EM (single particle) / Resolution: 12.8 Å

EMDB-2230:
The architecture of human general transcription factor TFIID core complex
Method: EM (single particle) / Resolution: 11.6 Å

EMDB-2231:
The architecture of human general transcription factor TFIID core complex
Method: EM (single particle) / Resolution: 14.3 Å

Source
  • Homo sapiens (human)

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