Molecular structure of promoter-bound yeast TFIID

Olga Kolesnikova, Adam Ben-Shem, Jie Luo, Jeff Ranish, Patrick Schultz () and Gabor Papai ()
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Olga Kolesnikova: Institut de Génétique et de Biologie Moléculaire et Cellulaire
Adam Ben-Shem: Institut de Génétique et de Biologie Moléculaire et Cellulaire
Jie Luo: Institute for Systems Biology
Jeff Ranish: Institute for Systems Biology
Patrick Schultz: Institut de Génétique et de Biologie Moléculaire et Cellulaire
Gabor Papai: Institut de Génétique et de Biologie Moléculaire et Cellulaire

Nature Communications, 2018, vol. 9, issue 1, 1-10

Abstract: Abstract 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 TBP-associate 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.

Date: 2018
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DOI: 10.1038/s41467-018-07096-y

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