EMD-0255
Molecular structure of promoter-bound yeast TFIID (locally-refined Twin lobe)
EMD-0255
Single-particle4.8 Å
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Map released: 21/11/2018
Last modified: 25/11/2020
Sample Organism:
Komagataella phaffii GS115
Sample: Transcription Factor IID
Deposition Authors: Kolesnikova O, Ben-Shem A, Luo J, Ranish J, Schultz P, Papai G
Sample: Transcription Factor IID
Deposition Authors: Kolesnikova O, Ben-Shem A, Luo J, Ranish J, Schultz P, Papai G
Molecular structure of promoter-bound yeast TFIID.
Kolesnikova O
,
Ben-Shem A
,
Luo J
,
Ranish J
,
Schultz P
,
Papai G
(2018) Nat Commun , 9 , 4666 - 4666
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(2018) Nat Commun , 9 , 4666 - 4666
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.
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.