title: Structure of promoter-bound TFIID and model of human pre-initiation complex assembly.
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.
authors.affiliation: Biophysics Graduate Group, University of California, Berkeley, California 94720, USA.
authors.forename: Robert K
authors.initials: RK
authors.lastname: Louder
authors.affiliation: QB3 Institute, Department of Molecular and Cell Biology, University of California, Berkeley, California 94720, USA.|Molecular Biophysics and Integrative Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA.
authors.forename: Yuan
authors.initials: Y
authors.lastname: He
authors.affiliation: Department of Biological Physical Chemistry, Rocasolano Physical Chemistry Institute, CSIC, Serrano 119, Madrid 28006, Spain.
authors.forename: José Ramón
authors.initials: JR
authors.lastname: López-Blanco
authors.affiliation: Howard Hughes Medical Institute, University of California, Berkeley, California 94720, USA.
authors.forename: Jie
authors.initials: J
authors.lastname: Fang
authors.affiliation: Department of Biological Physical Chemistry, Rocasolano Physical Chemistry Institute, CSIC, Serrano 119, Madrid 28006, Spain.
authors.forename: Pablo
authors.initials: P
authors.lastname: Chacón
authors.affiliation: QB3 Institute, Department of Molecular and Cell Biology, University of California, Berkeley, California 94720, USA.|Molecular Biophysics and Integrative Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA.|Howard Hughes Medical Institute, University of California, Berkeley, California 94720, USA.
authors.forename: Eva
authors.initials: E
authors.lastname: Nogales
mesh_terms: D020285:Cryoelectron Microscopy; D004247:DNA / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure; D006801:Humans; D008958:Models, Molecular; D011401:Promoter Regions, Genetic / Q000235:genetics*; D011485:Protein Binding; D013379:Substrate Specificity; D016385:TATA Box / Q000235:genetics; D035381:TATA-Binding Protein Associated Factors / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure; D035181:TATA-Box Binding Protein / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure; D035561:Transcription Factor TFIIA / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure; D035362:Transcription Factor TFIID / Q000737:chemistry / Q000378:metabolism* / Q000648:ultrastructure*; D061785:Transcription Initiation, Genetic
chemical_list: D035381:TATA-Binding Protein Associated Factors; D035181:TATA-Box Binding Protein; D035561:Transcription Factor TFIIA; D035362:Transcription Factor TFIID; D004247:DNA