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Publication - Dr Anna Chambers

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

    Citation

    Gupta, K, Watson, AA, Baptista, T, Scheer, E, Chambers, AL, Koehler, C, Zou, J, Obong-Ebong, I, Kandiah, E, Temblador, A, Round, A, Forest, E, Man, P, Bieniossek, C, Laue, ED, Lemke, EA, Rappsilber, J, Robinson, CV, Devys, D, Tora, L & Berger, I, 2017, ‘Architecture of TAF11/TAF13/TBP complex suggests novel regulation properties of general transcription factor TFIID’. eLife, vol 6.

    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.

    Full details in the University publications repository