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.
journal_name
Nat Communjournal_title
Nature communicationsauthors
Kolesnikova O,Ben-Shem A,Luo J,Ranish J,Schultz P,Papai Gdoi
10.1038/s41467-018-07096-ysubject
Has Abstractpub_date
2018-11-07 00:00:00pages
4666issue
1issn
2041-1723pii
10.1038/s41467-018-07096-yjournal_volume
9pub_type
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