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, Imre Berger

Research output: Contribution to journalArticlepeer-review

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.

Original languageEnglish
Article number6011
JournalNature Communications
Volume6
DOIs
Publication statusPublished - 1 Jan 2015

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