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

Kapil Gupta, Aleksandra A Watson, Tiago Baptista, Elisabeth Scheer, Anna L Chambers, Christine Koehler, Juan Zou, Ima Obong-Ebong, Eaazhisai Kandiah, Arturo Temblador, Adam Round, Eric Forest, Petr Man, Christoph Bieniossek, Ernest D Laue, Edward A Lemke, Juri Rappsilber, Carol V Robinson, Didier Devys, Làszlò ToraImre Berger

Research output: Contribution to journalArticle (Academic Journal)

19 Citations (Scopus)
436 Downloads (Pure)

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 languageEnglish
Article numbere30395
Number of pages31
JournaleLife
Volume6
DOIs
Publication statusPublished - 16 Nov 2017

Structured keywords

  • Bristol BioDesign Institute

Keywords

  • SYNTHETIC BIOLOGY

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