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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.

SUBMITTER: Kolesnikova O

PROVIDER: S-EPMC6220335 | biostudies-literature | 2018 Nov

REPOSITORIES: biostudies-literature

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Molecular structure of promoter-bound yeast TFIID.

Kolesnikova Olga O Ben-Shem Adam A Luo Jie J Ranish Jeff J Schultz Patrick P Papai Gabor G

Nature communications 20181107 1

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 stu ...[more]

PMID: 30405110

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