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-Structure paper
Title | Mapping the deubiquitination module within the SAGA complex. |
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Journal, issue, pages | Structure, Vol. 22, Issue 11, Page 1553-1559, Year 2014 |
Publish date | Nov 4, 2014 |
PubMed Abstract | The molecular organization of the yeast transcriptional coactivator Spt-Ada-Gcn5 acetyltransferase (SAGA) was analyzed by single-particle electron microscopy. Complete or partial deletion of the ...The molecular organization of the yeast transcriptional coactivator Spt-Ada-Gcn5 acetyltransferase (SAGA) was analyzed by single-particle electron microscopy. Complete or partial deletion of the Sgf73 subunit disconnects the deubiquitination (DUB) module from SAGA and favors in our conditions the cleavage of the C-terminal ends of the Spt7 subunit and the loss of the Spt8 subunit. The structural comparison of the wild-type SAGA with two deletion mutants positioned the DUB module and enabled the fitting of the available atomic models. The localization of the DUB module close to Gcn5 defines a chromatin-binding interface within SAGA, which could be demonstrated by the binding of nucleosome core particles. The TATA-box binding protein (TBP)-interacting subunit Spt8 was found to be located close to the DUB but in a different domain than Spt3, also known to contact TBP. A flexible protein arm brings both subunits close enough to interact simultaneously with TBP. |
External links | Structure / PubMed:25441028 |
Methods | EM (single particle) |
Resolution | 25.8 - 30.3 Å |
Structure data | EMDB-2693: EMDB-2694: |
Source |
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