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Structure of promoter-bound TFIID and model of human pre-initiation complex assembly
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Structure of promoter-bound TFIID and model of human pre-initiation complex assembly
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Journal Article
Structure of promoter-bound TFIID and model of human pre-initiation complex assembly
2016
Overview
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.
A sub-nanometre resolution cryo-EM structure of human TFIID bound to TFIIA and core promoter DNA and a model of the TFIID-based pre-initiation complex.
Promoter-bound TFIID structure
This paper describes the interaction of the human general transcription factor IID (TFIID) with core promoter DNA. TFIID has a central role in the initiation of RNA polymerase II dependent transcription by nucleating assembly of the pre-initiation complex (PIC) at the promoter. Eva Nogales and colleagues determine a sub-nanometre resolution cryo-electron microscopy structure of TFIID bound to TFIIA and core promoter DNA. They also present a cryo-electron microscopy reconstruction of a fully assembled human PIC lacking TBP-associated factors (TAFs). By superimposing common elements between the TFIID–TFIIA–promoter structure and the TAF-less PIC structure, they propose a structural model for the complete TFIID-based PIC, and provide insights into the role of TFIID in promoter recognition, PIC assembly, and transcription initiation.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
/ Analysis
/ DNA
/ Humanities and Social Sciences
/ Humans
/ Identification and classification
/ Promoter Regions, Genetic - genetics
/ RNA
/ Science
/ Studies
/ TATA-Binding Protein Associated Factors - chemistry
/ TATA-Binding Protein Associated Factors - metabolism
/ TATA-Binding Protein Associated Factors - ultrastructure
/ TATA-Box Binding Protein - chemistry
/ TATA-Box Binding Protein - metabolism
/ TATA-Box Binding Protein - ultrastructure
/ Transcription Factor TFIIA - chemistry
/ Transcription Factor TFIIA - metabolism
/ Transcription Factor TFIIA - ultrastructure
/ Transcription Factor TFIID - chemistry
/ Transcription Factor TFIID - metabolism
