Structural similarity between TAFs and the heterotetrameric core of the histone octamer

@article{Xie1996StructuralSB,
  title={Structural similarity between TAFs and the heterotetrameric core of the histone octamer},
  author={Xiaoling Xie and Tetsuro Kokubo and Steven L. Cohen and Urooj A. Mirza and Alexander Hoffmann and Brian T. Chait and Robert G. Roeder and Yoshihiro Nakatani and Stephen K. Burley},
  journal={Nature},
  year={1996},
  volume={380},
  pages={316-322}
}
A complex of two TFIID TATA box-binding protein-associated factors (TAFIIs) is described at 2.0 Å resolution. The amino-terminal portions of dTAFII42 and dTAFII62 from Drosophila adopt the canonical histone fold, consisting of two short α-helices flanking a long central α-helix. Like histones H3 and H4, dTAFII42 and dTAFII62 form an intimate heterodimer by extensive hydrophobic contacts between the paired molecules. In solution and in the crystalline state, the dTAFII42/dTAFII62 complex exists… 
Molecular structure of promoter-bound yeast TFIID.
TLDR
The cryo-electron microscopy structure of promoter-bound yeast TFIID at a resolution better than 5 A, except for a flexible domain is presented and the unique subunit stoichiometry prevailing in TFIIDs is confirmed.
Crystal Structure of Negative Cofactor 2 Recognizing the TBP-DNA Transcription Complex
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
Three-dimensional structures of the TAFII-containing complexes TFIID and TFTC.
TLDR
The structures of TFIID and TFTC have been determined at 3.5-nanometer resolution by electron microscopy and digital image analysis of single particles.
Asymmetry in the burial of hydrophobic residues along the histone chains of Eukarya, Archaea and a transcription factor
TLDR
Calculations utilizing the X-ray structures at atomic resolution of a hyperthermophile from Methanopyrus kandleri and a eukaryotic transcription factor from Drosophila melanogaster, that are structurally homologous to the eUKaryotic (H3-H4)2 tetramer, find reduced burial of hydrophobic residues is found to parallel the burial at the c-terminal regions of the H3 histones.
Mapping histone fold TAFs within yeast TFIID
TLDR
Immunolabelling experiments showed that nine TAFs that contain the histone fold structural motif were located in three distinct substructures of TFIID, showing that the previously reported pair‐wise interactions between hist one fold domain (HFD)‐containing TAFS are likely to occur in the native yTFIID complex.
The TAFII250 Subunit of TFIID Has Histone Acetyltransferase Activity
Novel dimerization fold of RAP30/RAP74 in human TFIIF at 1.7 A resolution.
TLDR
The X-ray structure of the RAP30/RAP74 interaction domains reveals a novel "triple barrel" dimerization fold and suggests with mutant data that interactions with the transcription apparatus are mediated not only by this tripartite beta-barrel, but also via flexible loops and alpha and beta-structures extending from it.
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