Download MendeleyMolecular 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
- PubMed: 30405110
- DOI: https://doi.org/10.1038/s41467-018-07096-y
- Primary Citation of Related Structures:
6HQA - PubMed 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.
Organizational Affiliation:
Department of Integrated Structural Biology, Equipe labellisée Ligue Contre le Cancer, Institut de Génétique et de Biologie Moléculaire et Cellulaire, Illkirch, 67404, France.
