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Structure paper

TitleStructure of the transcription coactivator SAGA.
Journal, issue, pagesNature, Vol. 577, Issue 7792, Page 717-720, Year 2020
Publish dateJan 22, 2020
AuthorsHaibo Wang / Christian Dienemann / Alexandra Stützer / Henning Urlaub / Alan C M Cheung / Patrick Cramer /
PubMed AbstractGene transcription by RNA polymerase II is regulated by activator proteins that recruit the coactivator complexes SAGA (Spt-Ada-Gcn5-acetyltransferase) and transcription factor IID (TFIID). SAGA is ...Gene transcription by RNA polymerase II is regulated by activator proteins that recruit the coactivator complexes SAGA (Spt-Ada-Gcn5-acetyltransferase) and transcription factor IID (TFIID). SAGA is required for all regulated transcription and is conserved among eukaryotes. SAGA contains four modules: the activator-binding Tra1 module, the core module, the histone acetyltransferase (HAT) module and the histone deubiquitination (DUB) module. Previous studies provided partial structures, but the structure of the central core module is unknown. Here we present the cryo-electron microscopy structure of SAGA from the yeast Saccharomyces cerevisiae and resolve the core module at 3.3 Å resolution. The core module consists of subunits Taf5, Sgf73 and Spt20, and a histone octamer-like fold. The octamer-like fold comprises the heterodimers Taf6-Taf9, Taf10-Spt7 and Taf12-Ada1, and two histone-fold domains in Spt3. Spt3 and the adjacent subunit Spt8 interact with the TATA box-binding protein (TBP). The octamer-like fold and its TBP-interacting region are similar in TFIID, whereas Taf5 and the Taf6 HEAT domain adopt distinct conformations. Taf12 and Spt20 form flexible connections to the Tra1 module, whereas Sgf73 tethers the DUB module. Binding of a nucleosome to SAGA displaces the HAT and DUB modules from the core-module surface, allowing the DUB module to bind one face of an ubiquitinated nucleosome.
External linksNature / PubMed:31969703 / PubMed Central
MethodsEM (single particle)
Resolution3.3 - 6.1 Å
Structure data

10412

6t9i

EMDB-10412, PDB-6t9i:
cryo-EM structure of transcription coactivator SAGA
Method: EM (single particle) / Resolution: 3.9 Å

10413

6t9j

EMDB-10413, PDB-6t9j:
SAGA Tra1 module
Method: EM (single particle) / Resolution: 3.4 Å

10414

6t9k

EMDB-10414, PDB-6t9k:
SAGA Core module
Method: EM (single particle) / Resolution: 3.3 Å

10415

6t9l

EMDB-10415, PDB-6t9l:
SAGA DUB module bound to a ubiqitinated nucleosome
Method: EM (single particle) / Resolution: 3.6 Å

EMDB-10416:
nucleosome-bound state of SAGA coactivator
Method: EM (single particle) / Resolution: 6.1 Å

Chemicals

ChemComp-ZN:
Unknown entry

Source
  • saccharomyces cerevisiae s288c (yeast)
  • saccharomyces cerevisiae (strain atcc 204508 / s288c) (yeast)
  • xenopus laevis (African clawed frog)
  • synthetic construct (others)
  • homo sapiens (human)
KeywordsGENE REGULATION / Coactivator / Transcription / Histone acetyltransferase / Histone deubiquitinase

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