Cryo-EM reveals promoter DNA binding and conformational flexibility of the general transcription factor TFIID.
The general transcription factor IID (TFIID) is required for initiation of RNA polymerase II-dependent transcription at many eukaryotic promoters. TFIID comprises the TATA-binding protein (TBP) and several conserved TBP-associated factors (TAFs). Recognition of the core promoter by TFIID assists assembly of the preinitiation complex. Using cryo-electron microscopy in combination with methods for ab initio single-particle reconstruction and heterogeneity analysis, we have produced density maps of two conformational states of Schizosaccharomyces pombe TFIID, containing and lacking TBP. We report that TBP-binding is coupled to a massive histone-fold domain rearrangement. Moreover, docking of the TBP-TAF1(N-terminus) atomic structure to the TFIID map and reconstruction of a TAF-promoter DNA complex helps to account for TAF-dependent regulation of promoter-TBP and promoter-TAF interactions.
Elmlund
Hans
H
Department of Structural Biology, Fairchild Building, Stanford University School of Medicine, Stanford, CA 94305, USA. hael@stanford.edu
Baraznenok
Vera
V
Linder
Tomas
T
Szilagyi
Zsolt
Z
Rofougaran
Reza
R
Hofer
Anders
A
Hebert
Hans
H
Lindahl
Martin
M
Gustafsson
Claes M
CM
D020285:Cryoelectron Microscopy; D004247:DNA / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure; D008958:Models, Molecular; D046912:Multiprotein Complexes / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure; D011401:Promoter Regions, Genetic / Q000235:genetics / Q000502:physiology; D011487:Protein Conformation; D012568:Schizosaccharomyces / Q000737:chemistry*; D035181:TATA-Box Binding Protein / Q000378:metabolism; D035362:Transcription Factor TFIID / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure
D046912:Multiprotein Complexes; D035181:TATA-Box Binding Protein; D035362:Transcription Factor TFIID; D004247:DNA