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Nat Commun. 2018 Nov 7;9(1):4666. doi: 10.1038/s41467-018-07096-y.

Molecular structure of promoter-bound yeast TFIID.

Kolesnikova O1,2,3,4, Ben-Shem A1,2,3,4, Luo J5, Ranish J5, Schultz P6,7,8,9, Papai G10,11,12,13.

Author information

1
Department of Integrated Structural Biology, Equipe labellisée Ligue Contre le Cancer, Institut de Génétique et de Biologie Moléculaire et Cellulaire, Illkirch, 67404, France.
2
Centre National de la Recherche Scientifique, UMR7104, 67404, Illkirch, France.
3
Institut National de la Santé et de la Recherche Médicale, U1258, 67404, Illkirch, France.
4
Université de Strasbourg, Illkirch, 67404, France.
5
Institute for Systems Biology, Seattle, WA, 98109, USA.
6
Department of Integrated Structural Biology, Equipe labellisée Ligue Contre le Cancer, Institut de Génétique et de Biologie Moléculaire et Cellulaire, Illkirch, 67404, France. patrick.schultz@igbmc.fr.
7
Centre National de la Recherche Scientifique, UMR7104, 67404, Illkirch, France. patrick.schultz@igbmc.fr.
8
Institut National de la Santé et de la Recherche Médicale, U1258, 67404, Illkirch, France. patrick.schultz@igbmc.fr.
9
Université de Strasbourg, Illkirch, 67404, France. patrick.schultz@igbmc.fr.
10
Department of Integrated Structural Biology, Equipe labellisée Ligue Contre le Cancer, Institut de Génétique et de Biologie Moléculaire et Cellulaire, Illkirch, 67404, France. gabor.papai@igbmc.fr.
11
Centre National de la Recherche Scientifique, UMR7104, 67404, Illkirch, France. gabor.papai@igbmc.fr.
12
Institut National de la Santé et de la Recherche Médicale, U1258, 67404, Illkirch, France. gabor.papai@igbmc.fr.
13
Université de Strasbourg, Illkirch, 67404, France. gabor.papai@igbmc.fr.

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.

PMID:
30405110
PMCID:
PMC6220335
DOI:
10.1038/s41467-018-07096-y
[Indexed for MEDLINE]
Free PMC Article

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