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Journal Articles Nature Communications Year : 2018

Molecular structure of promoter-bound yeast TFIID


Transcription preinitiation complex assembly on the promoters of protein encoding genes is nucleated in vivo by TFIID composed of the TATA-box Binding Protein (TBP) and 13 TBPassociate factors (Tafs) providing regulatory and chromatin binding functions. Here we present the cryo-electron microscopy structure of promoter-bound yeast TFIID at a resolution better than 5 Å, except for a flexible domain. We position the crystal structures of several subunits and, in combination with cross-linking studies, describe the quaternary organization of TFIID. The compact tri lobed architecture is stabilized by a topologically closed Taf5-Taf6 tetramer. We confirm the unique subunit stoichiometry prevailing in TFIID and uncover a hexameric arrangement of Tafs containing a histone fold domain in the Twin lobe.
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hal-02342125 , version 1 (04-01-2021)



Olga Kolesnikova, Adam Ben-Shem, Jie Luo, Jeff Ranish, Patrick Schultz, et al.. Molecular structure of promoter-bound yeast TFIID. Nature Communications, 2018, 9 (1), ⟨10.1038/s41467-018-07096-y⟩. ⟨hal-02342125⟩
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