Architecture of TAF11/TAF13/TBP complex suggests novel regulation properties of general transcription factor TFIID
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.
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Funding
Wellcome
- Imre Berger
H2020 European Research Council (ERC-2013-340551)
- Làszlò Tora
Research Councils UK
- Imre Berger
Agence Nationale de la Recherche (ANR-13-BSV8-0021-03)
- Imre Berger
Baden-Württemberg Stiftung
- Imre Berger
The funders had no role in study design, data collection and interpretation, or the decision to submit the work for publication.
Reviewing Editor
- Cynthia Wolberger, Johns Hopkins University, United States
Version history
- Received: July 13, 2017
- Accepted: November 3, 2017
- Accepted Manuscript published: November 7, 2017 (version 1)
- Version of Record published: November 16, 2017 (version 2)
Copyright
© 2017, Gupta et al.
This article is distributed under the terms of the Creative Commons Attribution License permitting unrestricted use and redistribution provided that the original author and source are credited.
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