Activities per year
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.
Original language | English |
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Article number | e30395 |
Number of pages | 31 |
Journal | eLife |
Volume | 6 |
DOIs | |
Publication status | Published - 16 Nov 2017 |
Research Groups and Themes
- Bristol BioDesign Institute
Keywords
- SYNTHETIC BIOLOGY
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Dive into the research topics of 'Architecture of TAF11/TAF13/TBP complex suggests novel regulation properties of general transcription factor TFIID'. Together they form a unique fingerprint.Activities
- 1 Fellowship awarded competitively
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Career Development Fellowship - The function of the Irc5 subfamily of chromatin remodelling enzymes in DNA repair.
Chambers, A. L. (Recipient)
1 Oct 2014 → 1 Oct 2017Activity: Other activity types › Fellowship awarded competitively