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Elife. 2017 Nov 7;6. pii: e30395. doi: 10.7554/eLife.30395.

Architecture of TAF11/TAF13/TBP complex suggests novel regulation properties of general transcription factor TFIID.

Author information

1
BrisSynBio Centre, The School of Biochemistry, Faculty of Biomedical Sciences, University of Bristol, Bristol, United Kingdom.
2
European Molecular Biology Laboratory, Grenoble, France.
3
Department of Biochemistry, University of Cambridge, Cambridge, United Kingdom.
4
Institut de Génétique et de Biologie Moléculaire et Cellulaire IGBMC, Illkirch, France.
5
Centre National de la Recherche Scientifique, Illkirch, France.
6
Institut National de la Santé et de la Recherche Médicale, Illkirch, France.
7
Université de Strasbourg, Illkirch, France.
8
European Molecular Biology Laboratory, Heidelberg, Germany.
9
Wellcome Trust Centre for Cell Biology, University of Edinburgh, Edinburgh, United Kingdom.
10
Chair of Bioanalytics, Institute of Biotechnology, Technische Universität Berlin, Berlin, Germany.
11
Physical and Theoretical Chemistry Laboratory, Oxford, United Kingdom.
12
Institut de Biologie Structurale IBS, Grenoble, France.
13
Institute of Microbiology, The Czech Academy of Sciences, Vestec, Czech Republic.
14
BioCeV - Faculty of Science, Charles University, Prague, Czech Republic.

Abstract

General transcription factor TFIID is a key component of RNA polymerase II transcription initiation. Human TFIID is a megadalton-sized complex comprising TATA-binding protein (TBP) and 13 TBP-associated factors (TAFs). TBP binds to core promoter DNA, recognizing the TATA-box. We identified a ternary complex formed by TBP and the histone fold (HF) domain-containing TFIID subunits TAF11 and TAF13. We demonstrate that TAF11/TAF13 competes for TBP binding with TATA-box DNA, and also with the N-terminal domain of TAF1 previously implicated in TATA-box mimicry. In an integrative approach combining crystal coordinates, biochemical analyses and data from cross-linking mass-spectrometry (CLMS), we determine the architecture of the TAF11/TAF13/TBP complex, revealing TAF11/TAF13 interaction with the DNA binding surface of TBP. We identify a highly conserved C-terminal TBP-interaction domain (CTID) in TAF13, which is essential for supporting cell growth. Our results thus have implications for cellular TFIID assembly and suggest a novel regulatory state for TFIID function.

KEYWORDS:

S. cerevisiae; TBP associated factors; TFIID; biochemistry; biophysics; core promoter DNA; gene regulation; histone fold domain; human; structural biology; transcription factors

PMID:
29111974
PMCID:
PMC5690282
DOI:
10.7554/eLife.30395
[Indexed for MEDLINE]
Free PMC Article

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