1. Academic Validation
  2. Structure of promoter-bound TFIID and model of human pre-initiation complex assembly

Structure of promoter-bound TFIID and model of human pre-initiation complex assembly

  • Nature. 2016 Mar 31;531(7596):604-9. doi: 10.1038/nature17394.
Robert K Louder 1 Yuan He 2 3 José Ramón López-Blanco 4 Jie Fang 5 Pablo Chacón 4 Eva Nogales 2 3 5
Affiliations

Affiliations

  • 1 Biophysics Graduate Group, University of California, Berkeley, California 94720, USA.
  • 2 QB3 Institute, Department of Molecular and Cell Biology, University of California, Berkeley, California 94720, USA.
  • 3 Molecular Biophysics and Integrative Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA.
  • 4 Department of Biological Physical Chemistry, Rocasolano Physical Chemistry Institute, CSIC, Serrano 119, Madrid 28006, Spain.
  • 5 Howard Hughes Medical Institute, University of California, Berkeley, California 94720, USA.
Abstract

The general transcription factor IID (TFIID) plays a central role in the initiation of RNA polymerase II (Pol II)-dependent transcription by nucleating pre-initiation complex (PIC) assembly at the core promoter. TFIID comprises the TATA-binding protein (TBP) and 13 TBP-associated factors (TAF1-13), which specifically interact with a variety of core promoter DNA sequences. Here we present the structure of human TFIID in complex with TFIIA and core promoter DNA, determined by single-particle cryo-electron microscopy at sub-nanometre resolution. All core promoter elements are contacted by subunits of TFIID, with TAF1 and TAF2 mediating major interactions with the downstream promoter. TFIIA bridges the TBP-TATA complex with lobe B of TFIID. We also present the cryo-electron microscopy reconstruction of a fully assembled human TAF-less PIC. Superposition of common elements between the two structures provides novel insights into the general role of TFIID in promoter recognition, PIC assembly, and transcription initiation.

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