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Publication Abstract from PubMed

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 A, 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.

Molecular structure of promoter-bound yeast TFIID.,Kolesnikova O, Ben-Shem A, Luo J, Ranish J, Schultz P, Papai G Nat Commun. 2018 Nov 7;9(1):4666. doi: 10.1038/s41467-018-07096-y. PMID:30405110^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.