Architecture of TAF11/TAF13/TBP complex suggests novel regulation properties of general transcription factor TFIID - Archive ouverte HAL Access content directly
Journal Articles eLife Year : 2017

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

Eric Forest
  • Function : Author
  • PersonId : 860133

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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Dates and versions

hal-01647012 , version 1 (04-01-2024)

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Kapil Gupta, Aleksandra A Watson, Tiago Baptista, Elisabeth Scheer, Anna L Chambers, et al.. Architecture of TAF11/TAF13/TBP complex suggests novel regulation properties of general transcription factor TFIID. eLife, 2017, 6, ⟨10.7554/eLife.30395⟩. ⟨hal-01647012⟩
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