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

Article

关键词: RNA-POLYMERASE-II;    TATA-BINDING PROTEIN;    CORE PROMOTER;    TRANSCRIPTION INITIATION;    ELECTRON-MICROSCOPY;    CRYSTAL-STRUCTURE;    HUMAN GENOME;    CRYO-EM;    TAFS;    ARCHITECTURE;   

DOI  :  10.1038/nature17394

来源: SCIE

【 摘 要 】

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.

【 授权许可】

Free