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    Investigating the yeast Spt-Ada-Gcn5 acetyltransferase (SAGA) complex using electron microscopy revealed its molecular organization. Deleting Sgf73 destabilizes the deubiquitination module and affects other subunits, impacting SAGA

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    Area of Science:

    • Molecular biology
    • Structural biology
    • Yeast genetics

    Background:

    • The Spt-Ada-Gcn5 acetyltransferase (SAGA) complex is a crucial transcriptional coactivator in yeast.
    • Understanding SAGA's molecular organization is key to elucidating its regulatory functions in gene expression.

    Purpose of the Study:

    • To determine the molecular organization of the yeast SAGA complex.
    • To investigate the structural role of the Sgf73 subunit and its impact on SAGA integrity.
    • To map the localization of the deubiquitination (DUB) module and its interaction interfaces within SAGA.

    Main Methods:

    • Single-particle electron microscopy was employed to analyze the wild-type and mutant SAGA complexes.
    • Structural comparisons were made between wild-type SAGA and deletion mutants lacking Sgf73.
    • Nucleosome core particles were used to demonstrate the chromatin-binding interface of SAGA.

    Main Results:

    • Complete or partial deletion of the Sgf73 subunit disconnects the DUB module from SAGA.
    • Sgf73 deletion favors C-terminal cleavage of Spt7 and loss of Spt8.
    • The DUB module localizes near Gcn5, forming a chromatin-binding interface.
    • Spt8 and Spt3 subunits, both interacting with TATA-binding protein (TBP), are positioned to interact simultaneously with TBP via a flexible arm.

    Conclusions:

    • The Sgf73 subunit is essential for maintaining the structural integrity of the SAGA complex, particularly the DUB module.
    • SAGA possesses a defined chromatin-binding interface involving the DUB module and Gcn5.
    • The structural arrangement facilitates simultaneous interaction of SAGA with TBP through distinct subunits.