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  Structure of the transcription coactivator SAGA.

Wang, H., Dienemann, C., Stützer, A., Urlaub, H., Cheung, A. C. M., & Cramer, P. (2020). Structure of the transcription coactivator SAGA. Nature, 577, 717-720. doi:10.1038/s41586-020-1933-5.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0005-8B4D-9 Version Permalink: http://hdl.handle.net/21.11116/0000-0005-B7F9-4
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 Creators:
Wang, H.1, Author              
Dienemann, C.1, Author              
Stützer, A.2, Author              
Urlaub, H.3, Author              
Cheung, A. C. M., Author
Cramer, P.1, Author              
Affiliations:
1Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society, ou_1863498              
2Research Group of Chromatin Biochemistry, MPI for biochemical chemistry, Max Planck Society, ou_578604              
3Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society, ou_578613              

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 Abstract: Gene transcription by RNA polymerase II is regulated by activator proteins that recruit the coactivator complexes SAGA (Spt-Ada-Gcn5-acetyltransferase)1,2 and transcription factor IID (TFIID)2-4. SAGA is required for all regulated transcription5 and is conserved among eukaryotes6. SAGA contains four modules7-9: the activator-binding Tra1 module, the core module, the histone acetyltransferase (HAT) module and the histone deubiquitination (DUB) module. Previous studies provided partial structures10-14, 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)2,7,15-17. 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.

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Language(s): eng - English
 Dates: 2020-01-222020
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1038/s41586-020-1933-5
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Title: Nature
Source Genre: Journal
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Pages: - Volume / Issue: 577 Sequence Number: - Start / End Page: 717 - 720 Identifier: -