4OY2

Crystal structure of TAF1-TAF7, a TFIID subcomplex

4OY2 の概要

• エントリーDOI: 10.2210/pdb4oy2/pdb
• 分子名称: Transcription initiation factor TFIID subunit 1, Transcription initiation factor TFIID subunit 7, ZINC ION, ... (5 entities in total)
• 機能のキーワード: taf1, taf7, tfiid, rna pol ii initiation factors, transcription
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 258635.17

構造登録者

Bhattacharya, S.,Lou, X.,Rajashankar, K.,Jacobson, R.H.,Webb, P. (登録日: 2014-02-10, 公開日: 2014-06-25, 最終更新日: 2024-11-20)

主引用文献

Bhattacharya, S.,Lou, X.,Hwang, P.,Rajashankar, K.R.,Wang, X.,Gustafsson, J.-A.,Fletterick, R.J.,Jacobson, R.H.,Webb, P.
Structural and functional insight into TAF1-TAF7, a subcomplex of transcription factor II D.
Proc.Natl.Acad.Sci.USA, 111:9103-9108, 2014

PubMed Abstract: Transcription factor II D (TFIID) is a multiprotein complex that nucleates formation of the basal transcription machinery. TATA binding protein-associated factors 1 and 7 (TAF1 and TAF7), two subunits of TFIID, are integral to the regulation of eukaryotic transcription initiation and play key roles in preinitiation complex (PIC) assembly. Current models suggest that TAF7 acts as a dissociable inhibitor of TAF1 histone acetyltransferase activity and that this event ensures appropriate assembly of the RNA polymerase II-mediated PIC before transcriptional initiation. Here, we report the 3D structure of a complex of yeast TAF1 with TAF7 at 2.9 Å resolution. The structure displays novel architecture and is characterized by a large predominantly hydrophobic heterodimer interface and extensive cofolding of TAF subunits. There are no obvious similarities between TAF1 and known histone acetyltransferases. Instead, the surface of the TAF1-TAF7 complex contains two prominent conserved surface pockets, one of which binds selectively to an inhibitory trimethylated histone H3 mark on Lys27 in a manner that is also regulated by phosphorylation at the neighboring H3 serine. Our findings could point toward novel roles for the TAF1-TAF7 complex in regulation of PIC assembly via reading epigenetic histone marks.

PubMed: 24927529
DOI: 10.1073/pnas.1408293111

実験手法

X-RAY DIFFRACTION (2.9 Å)