Cytoplasmic TAF2–TAF8–TAF10 complex provides evidence for nuclear holo–TFIID assembly from preformed submodules

Simon Trowitzsch, Cristina Viola, Elisabeth Scheer, Sascha Conic, Virginie Chavant, Marjorie Fournier, Gabor Papai, Ima-Obong Ebong, Christiane Schaffitzel, Juan Zou, Matthias Haffke, Juri Rappsilber, Carol V. Robinson, Patrick Schultz, Laszlo Tora () and Imre Berger ()
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Simon Trowitzsch: European Molecular Biology Laboratory, Grenoble Outstation
Cristina Viola: European Molecular Biology Laboratory, Grenoble Outstation
Elisabeth Scheer: Cellular Signaling and Nuclear Dynamics Program, Institut de Génétique et de Biologie Moléculaire et Cellulaire
Sascha Conic: Cellular Signaling and Nuclear Dynamics Program, Institut de Génétique et de Biologie Moléculaire et Cellulaire
Virginie Chavant: Proteomics Platform, Institut de Génétique et de Biologie Moléculaire et Cellulaire
Marjorie Fournier: Cellular Signaling and Nuclear Dynamics Program, Institut de Génétique et de Biologie Moléculaire et Cellulaire
Gabor Papai: Institut de Génétique et de Biologie Moléculaire et Cellulaire
Ima-Obong Ebong: Chemistry Research Laboratory, University of Oxford
Christiane Schaffitzel: European Molecular Biology Laboratory, Grenoble Outstation
Juan Zou: Wellcome Trust Centre for Cell Biology, University of Edinburgh
Matthias Haffke: European Molecular Biology Laboratory, Grenoble Outstation
Juri Rappsilber: Wellcome Trust Centre for Cell Biology, University of Edinburgh
Carol V. Robinson: Chemistry Research Laboratory, University of Oxford
Patrick Schultz: Institut de Génétique et de Biologie Moléculaire et Cellulaire
Laszlo Tora: Cellular Signaling and Nuclear Dynamics Program, Institut de Génétique et de Biologie Moléculaire et Cellulaire
Imre Berger: European Molecular Biology Laboratory, Grenoble Outstation

Nature Communications, 2015, vol. 6, issue 1, 1-14

Abstract: Abstract General transcription factor TFIID is a cornerstone of RNA polymerase II transcription initiation in eukaryotic cells. How human TFIID—a megadalton-sized multiprotein complex composed of the TATA-binding protein (TBP) and 13 TBP-associated factors (TAFs)—assembles into a functional transcription factor is poorly understood. Here we describe a heterotrimeric TFIID subcomplex consisting of the TAF2, TAF8 and TAF10 proteins, which assembles in the cytoplasm. Using native mass spectrometry, we define the interactions between the TAFs and uncover a central role for TAF8 in nucleating the complex. X-ray crystallography reveals a non-canonical arrangement of the TAF8–TAF10 histone fold domains. TAF2 binds to multiple motifs within the TAF8 C-terminal region, and these interactions dictate TAF2 incorporation into a core–TFIID complex that exists in the nucleus. Our results provide evidence for a stepwise assembly pathway of nuclear holo–TFIID, regulated by nuclear import of preformed cytoplasmic submodules.

Date: 2015
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DOI: 10.1038/ncomms7011

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