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

Robert K. Louder, Yuan He, José Ramón López-Blanco, Jie Fang, Pablo Chacón and Eva Nogales ()
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Robert K. Louder: Biophysics Graduate Group, University of California, Berkeley
Yuan He: QB3 Institute, University of California
José Ramón López-Blanco: Rocasolano Physical Chemistry Institute
Jie Fang: Howard Hughes Medical Institute, University of California
Pablo Chacón: Rocasolano Physical Chemistry Institute
Eva Nogales: QB3 Institute, University of California

Nature, 2016, vol. 531, issue 7596, 604-609

Abstract: 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.

Date: 2016
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DOI: 10.1038/nature17394

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