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Structure of the human SAGA coactivator complex.

Dominik A Herbst^1,2, Meagan N Esbin^3,4, Robert K Louder^1,4,5

¹California Institute for Quantitative Biology (QB3), University of California, Berkeley, CA, USA.

Nature Structural & Molecular Biology

|November 23, 2021

Summary

The human SAGA complex structure reveals significant differences from yeast, featuring a distinct organization and a metazoan-specific splicing module. This provides a framework for developing drugs targeting developmental diseases and cancer.

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Area of Science:

Molecular Biology
Structural Biology
Biochemistry

Background:

The SAGA complex is a crucial regulator of gene expression, chromatin modification, DNA repair, and signaling pathways.
While the structure of yeast SAGA (ySAGA) is known, significant functional and compositional differences exist in metazoan SAGA (hSAGA).

Purpose of the Study:

To determine the cryogenic-electron microscopy (cryo-EM) structure of human SAGA (hSAGA).
To elucidate the structural divergence of hSAGA compared to ySAGA and identify metazoan-specific features.
To provide a structural basis for understanding hSAGA function in human diseases and for drug design.

Main Methods:

Cryogenic-electron microscopy (cryo-EM) for high-resolution structural determination of hSAGA.
Comparative structural analysis between hSAGA and ySAGA.
Mapping of human disease mutations onto the hSAGA structure.

Main Results:

The hSAGA structure reveals a globally divergent organization compared to ySAGA, with a unique interface connecting the core module and TRRAP subunit.
A metazoan-specific splicing module is integrated into hSAGA.
An inositol hexakisphosphate (InsP6) binding site in TRRAP and an unusual property of its pseudo-(Ψ)PIKK were identified.

Conclusions:

The determined hSAGA structure highlights significant evolutionary divergence from yeast, impacting functional element geometry and incorporating a novel splicing module.
The structural insights, including the InsP6 binding site and disease mutation mapping, offer a foundation for structure-guided drug development for human diseases and cancer.