Journal
ELIFE
Volume 6, Issue -, Pages -Publisher
ELIFE SCIENCES PUBLICATIONS LTD
DOI: 10.7554/eLife.30395
Keywords
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Categories
Funding
- Baden-Wurttemberg Stiftung
- Wellcome Trust [10313]
- H European Research Council [ERC-2013-340551]
- Agence Nationale de la Recherche [ANR-13-BSV8-0021-03]
- Wellcome Trust
- Research Councils UK
- Wellcome Trust [103139/Z/13/Z] Funding Source: Wellcome Trust
- Agence Nationale de la Recherche (ANR) [ANR-13-BSV8-0021] Funding Source: Agence Nationale de la Recherche (ANR)
- Biotechnology and Biological Sciences Research Council [BB/L01386X/1] Funding Source: researchfish
- Cancer Research UK [17506] Funding Source: researchfish
- Wellcome Trust [103139/Z/13/Z] Funding Source: researchfish
- BBSRC [BB/L01386X/1] Funding Source: UKRI
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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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