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TitleConformational landscape of the yeast SAGA complex as revealed by cryo-EM.
Journal, issue, pagesSci Rep, Vol. 12, Issue 1, Page 12306, Year 2022
Publish dateJul 19, 2022
AuthorsDiana Vasyliuk / Joeseph Felt / Ellen D Zhong / Bonnie Berger / Joseph H Davis / Calvin K Yip /
PubMed AbstractSpt-Ada-Gcn5-Acetyltransferase (SAGA) is a conserved multi-subunit complex that activates RNA polymerase II-mediated transcription by acetylating and deubiquitinating nucleosomal histones and by ...Spt-Ada-Gcn5-Acetyltransferase (SAGA) is a conserved multi-subunit complex that activates RNA polymerase II-mediated transcription by acetylating and deubiquitinating nucleosomal histones and by recruiting TATA box binding protein (TBP) to DNA. The prototypical yeast Saccharomyces cerevisiae SAGA contains 19 subunits that are organized into Tra1, core, histone acetyltransferase, and deubiquitination modules. Recent cryo-electron microscopy studies have generated high-resolution structural information on the Tra1 and core modules of yeast SAGA. However, the two catalytical modules were poorly resolved due to conformational flexibility of the full assembly. Furthermore, the high sample requirement created a formidable barrier to further structural investigations of SAGA. Here, we report a workflow for isolating/stabilizing yeast SAGA and preparing cryo-EM specimens at low protein concentration using a graphene oxide support layer. With this procedure, we were able to determine a cryo-EM reconstruction of yeast SAGA at 3.1 Å resolution and examine its conformational landscape with the neural network-based algorithm cryoDRGN. Our analysis revealed that SAGA adopts a range of conformations with its HAT module and central core in different orientations relative to Tra1.
External linksSci Rep / PubMed:35853968 / PubMed Central
MethodsEM (single particle)
Resolution2.9 - 3.2 Å
Structure data

EMDB-26792: Transcription co-activator SAGA
Method: EM (single particle) / Resolution: 3.1 Å

EMDB-26803: Cryo-EM structure of the SAGA Tra1 module
Method: EM (single particle) / Resolution: 2.9 Å

EMDB-26804: Cryo-EM structure of the SAGA core module
Method: EM (single particle) / Resolution: 3.2 Å

Source
  • Saccharomyces cerevisiae (brewer's yeast)

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