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-Structure paper
Title | Molecular structure of promoter-bound yeast TFIID. |
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Journal, issue, pages | Nat Commun, Vol. 9, Issue 1, Page 4666, Year 2018 |
Publish date | Nov 7, 2018 |
![]() | Olga Kolesnikova / Adam Ben-Shem / Jie Luo / Jeff Ranish / Patrick Schultz / Gabor Papai / ![]() ![]() |
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) ...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. |
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Methods | EM (single particle) |
Resolution | 4.5 - 12.13 Å |
Structure data | ![]() EMDB-0249: ![]() EMDB-0250: EMDB-0251, PDB-6hqa: ![]() EMDB-0253: ![]() EMDB-0254: ![]() EMDB-0255: |
Source |
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![]() | TRANSCRIPTION / Complex / Transcription initiation |