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

Research output: Contribution to journalArticle

  • 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
  • Imre Berger

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Original languageEnglish
Article number6011
JournalNature Communications
Publication statusPublished - 1 Jan 2015


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.

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