5OJS

Cryo-EM structure of the SAGA and NuA4 coactivator subunit Tra1

Summary for 5OJS

• Entry DOI: 10.2210/pdb5ojs/pdb
• EMDB information: 3824
• Descriptor: Transcription-associated protein 1 (1 entity in total)
• Functional Keywords: coactivator, pikk, saga, nua4, transcription
• Biological source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
• Total number of polymer chains: 1
• Total formula weight: 436527.28

Authors

Diaz-Santin, L.M.,Lukoyanova, N.,Aciyan, E.,Cheung, A.C.M. (deposition date: 2017-07-24, release date: 2017-08-09, Last modification date: 2024-05-15)

Primary citation

Diaz-Santin, L.M.,Lukoyanova, N.,Aciyan, E.,Cheung, A.C.
Cryo-EM structure of the SAGA and NuA4 coactivator subunit Tra1 at 3.7 angstrom resolution.
Elife, 6:-, 2017

PubMed Abstract: Coactivator complexes SAGA and NuA4 stimulate transcription by post-translationally modifying chromatin. Both complexes contain the Tra1 subunit, a highly conserved 3744-residue protein from the Phosphoinositide 3-Kinase-related kinase (PIKK) family and a direct target for multiple sequence-specific activators. We present the Cryo-EM structure of Tra1 to 3.7 Å resolution, revealing an extensive network of alpha-helical solenoids organized into a diamond ring conformation and is strikingly reminiscent of DNA-PKcs, suggesting a direct role for Tra1 in DNA repair. The structure was fitted into an existing SAGA EM reconstruction and reveals limited contact surfaces to Tra1, hence it does not act as a molecular scaffold within SAGA. Mutations that affect activator targeting are distributed across the Tra1 structure, but also cluster within the N-terminal Finger region, indicating the presence of an activator interaction site. The structure of Tra1 is a key milestone in deciphering the mechanism of multiple coactivator complexes.

PubMed: 28767037
DOI: 10.7554/eLife.28384

Experimental method

ELECTRON MICROSCOPY (3.7 Å)