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Updated: Jun 18, 2026

Single-Molecule Imaging of EWS-FLI1 Condensates Assembling on DNA
Published on: September 8, 2021
Cryo-EM reveals promoter DNA binding and conformational flexibility of the general transcription factor TFIID
Hans Elmlund1, Vera Baraznenok, Tomas Linder
1Department of Structural Biology, Fairchild Building, Stanford University School of Medicine, Stanford, CA 94305, USA. hael@stanford.edu
Abstract:
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.
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