Molecular structure of promoter-bound yeast TFIID.

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 Commun

journal_title

Nature communications

authors

Kolesnikova O,Ben-Shem A,Luo J,Ranish J,Schultz P,Papai G

doi

10.1038/s41467-018-07096-y

subject

Has Abstract

pub_date

2018-11-07 00:00:00

pages

4666

issue

1

issn

2041-1723

pii

10.1038/s41467-018-07096-y

journal_volume

9

pub_type

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