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

Kapil Gupta (1) , Aleksandra A Watson (2) , Tiago Baptista (3) , Elisabeth Scheer (4) , Anna L Chambers (5) , Christine Koehler (6) , Juan Zou (7) , Ima Obong-Ebong (8) , Eaazhisai Kandiah (9) , Arturo Temblador (1) , Adam Round (1) , Eric Forest (9) , Petr Man (10) , Christoph Bieniossek (1) , Ernest D Laue (2) , Edward A Lemke (6) , Juri Rappsilber (7) , Carol V Robinson (11) , Didier Devys (3) , László Tora (4) , Imre Berger (1)

1 EMBL - European Molecular Biology Laboratory [Grenoble]
2 Department of Biochemistry [Cambridge]
3 IGBMC - Institut de Génétique et de Biologie Moléculaire et Cellulaire
4 IGBMC - Institut de génétique et biologie moléculaire et cellulaire
5 BrisSynBio Centre, The School of Biochemistry
6 EMBL - European Molecular Biology Laboratory [Heidelberg]
7 Wellcome Trust Centre for Cell Biology
8 Physical and Theoretical ChemistryLaboratory
9 IBS - UMR 5075 - Institut de biologie structurale
10 MBU / CAS - Institute of Microbiology of the Czech Academy of Sciences [Prague, Czech Republic]
11 Department of Chemistry, University of Oxford

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.

Domaines: Biologie structurale [q-bio.BM]

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⟩