Molecular structure of promoter-bound yeast TFIID.
Fiche publication
Date publication
novembre 2018
Journal
Nature communications
Auteurs
Membres identifiés du Cancéropôle Est :
Dr SCHULTZ Patrick, Dr BEN SHEM Adam
Tous les auteurs :
Kolesnikova O, Ben-Shem A, Luo J, Ranish J, Schultz P, Papai G
Lien Pubmed
Résumé
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.
Référence
Nat Commun. 2018 Nov 7;9(1):4666